{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,22]],"date-time":"2026-06-22T10:09:58Z","timestamp":1782122998777,"version":"3.54.5"},"reference-count":238,"publisher":"Springer Science and Business Media LLC","issue":"7","license":[{"start":{"date-parts":[[2024,5,21]],"date-time":"2024-05-21T00:00:00Z","timestamp":1716249600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2024,5,21]],"date-time":"2024-05-21T00:00:00Z","timestamp":1716249600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Mol Cell Biochem"],"published-print":{"date-parts":[[2024,7]]},"DOI":"10.1007\/s11010-024-05032-x","type":"journal-article","created":{"date-parts":[[2024,5,21]],"date-time":"2024-05-21T08:01:31Z","timestamp":1716278491000},"page":"1627-1642","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Protein networking: nicotinic acetylcholine receptors and their protein\u2013protein-associations"],"prefix":"10.1007","volume":"479","author":[{"ORCID":"https:\/\/orcid.org\/0009-0008-4521-5474","authenticated-orcid":false,"given":"Sabrina","family":"Brockm\u00f6ller","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3531-3616","authenticated-orcid":false,"given":"Franz","family":"Worek","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2041-0034","authenticated-orcid":false,"given":"Simone","family":"Rothmiller","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2024,5,21]]},"reference":[{"key":"5032_CR1","doi-asserted-by":"publisher","first-page":"66","DOI":"10.1196\/annals.1254.009","volume":"998","author":"CP Wanamaker","year":"2003","unstructured":"Wanamaker CP, Christianson JC, Green WN (2003) Regulation of nicotinic acetylcholine receptor assembly. Ann N Y Acad Sci 998:66\u201380","journal-title":"Ann N Y Acad Sci"},{"key":"5032_CR2","doi-asserted-by":"publisher","first-page":"279","DOI":"10.1080\/09687680802035675","volume":"25","author":"NS Millar","year":"2008","unstructured":"Millar NS, Harkness PC (2008) Assembly and trafficking of nicotinic acetylcholine receptors (Review). Mol Membr Biol 25:279\u2013292. https:\/\/doi.org\/10.1080\/09687680802035675","journal-title":"Mol Membr Biol"},{"key":"5032_CR3","doi-asserted-by":"publisher","first-page":"73","DOI":"10.1152\/physrev.00015.2008","volume":"89","author":"EX Albuquerque","year":"2009","unstructured":"Albuquerque EX, Pereira EFR, Alkondon M et al (2009) Mammalian nicotinic acetylcholine receptors: from structure to function. Physiol Rev 89:73\u2013120. https:\/\/doi.org\/10.1152\/physrev.00015.2008","journal-title":"Physiol Rev"},{"key":"5032_CR4","doi-asserted-by":"publisher","first-page":"455","DOI":"10.1016\/j.tips.2010.07.001","volume":"31","author":"AK Jones","year":"2010","unstructured":"Jones AK, Buckingham SD, Sattelle DB (2010) Proteins interacting with nicotinic acetylcholine receptors: expanding functional and therapeutic horizons. Trends Pharmacol Sci 31:455\u2013462. https:\/\/doi.org\/10.1016\/j.tips.2010.07.001","journal-title":"Trends Pharmacol Sci"},{"key":"5032_CR5","doi-asserted-by":"publisher","first-page":"237","DOI":"10.1016\/j.neuropharm.2008.07.041","volume":"56","author":"NS Millar","year":"2009","unstructured":"Millar NS, Gotti C (2009) Diversity of vertebrate nicotinic acetylcholine receptors. Neuropharmacology 56:237\u2013246. https:\/\/doi.org\/10.1016\/j.neuropharm.2008.07.041","journal-title":"Neuropharmacology"},{"key":"5032_CR6","doi-asserted-by":"publisher","first-page":"2629","DOI":"10.1194\/jlr.M005132","volume":"51","author":"V Berm\u00fadez","year":"2010","unstructured":"Berm\u00fadez V, Antollini SS, Fern\u00e1ndez N et al (2010) Partition profile of the nicotinic acetylcholine receptor in lipid domains upon reconstitution. J Lipid Res 51:2629\u20132641. https:\/\/doi.org\/10.1194\/jlr.M005132","journal-title":"J Lipid Res"},{"key":"5032_CR7","doi-asserted-by":"publisher","first-page":"176","DOI":"10.1016\/S0166-2236(03)00066-3","volume":"26","author":"L Mei","year":"2003","unstructured":"Mei L, Xiong WC (2003) Two birds with one stone: a novel motif for ACh receptor assembly quality control. Trends Neurosci 26:176\u2013178. https:\/\/doi.org\/10.1016\/S0166-2236(03)00066-3","journal-title":"Trends Neurosci"},{"key":"5032_CR8","doi-asserted-by":"publisher","first-page":"967","DOI":"10.1016\/j.jmb.2004.12.031","volume":"346","author":"N Unwin","year":"2005","unstructured":"Unwin N (2005) Refined structure of the nicotinic acetylcholine receptor at 4 \u00c5 resolution. J Mol Biol 346:967\u2013989. https:\/\/doi.org\/10.1016\/j.jmb.2004.12.031","journal-title":"J Mol Biol"},{"key":"5032_CR9","doi-asserted-by":"publisher","first-page":"406","DOI":"10.1038\/321406a0","volume":"321","author":"M Mishina","year":"1986","unstructured":"Mishina M, Takai T, Imoto K et al (1986) Molecular distinction between fetal and adult forms of muscle acetylcholine receptor. Nature 321:406\u2013411","journal-title":"Nature"},{"key":"5032_CR10","doi-asserted-by":"publisher","first-page":"1244","DOI":"10.1097\/ALN.0b013e31819fade3","volume":"110","author":"MJ Fagerlund","year":"2009","unstructured":"Fagerlund MJ, Dabrowski M, Eriksson LI (2009) Pharmacological characteristics of the inhibition of nondepolarizing neuromuscular blocking agents at human adult muscle nicotinic acetylcholine receptor. J Am Soc Anesthesiol 110:1244\u20131252","journal-title":"J Am Soc Anesthesiol"},{"key":"5032_CR11","doi-asserted-by":"publisher","first-page":"57","DOI":"10.1016\/0092-8674(93)90294-Z","volume":"74","author":"WN Green","year":"1993","unstructured":"Green WN, Claudio T (1993) Acetylcholine receptor assembly: subunit folding and oligomerization occur sequentially. Cell 74:57\u201369","journal-title":"Cell"},{"key":"5032_CR12","doi-asserted-by":"publisher","first-page":"2771","DOI":"10.1523\/JNEUROSCI.10-08-02771.1990","volume":"10","author":"JR Forsayeth","year":"1990","unstructured":"Forsayeth JR, Franco A, Rossi AB et al (1990) Expression of functional mouse muscle acetylcholine receptors in Chinese hamster ovary cells. J Neurosci 10:2771\u20132779","journal-title":"J Neurosci"},{"key":"5032_CR13","doi-asserted-by":"publisher","first-page":"147","DOI":"10.1016\/0896-6273(90)90305-Y","volume":"5","author":"Y Gu","year":"1990","unstructured":"Gu Y, Franco A Jr, Gardner PD et al (1990) Properties of embryonic and adult muscle acetylcholine receptors transiently expressed in COS cells. Neuron 5:147\u2013157","journal-title":"Neuron"},{"key":"5032_CR14","doi-asserted-by":"publisher","first-page":"203","DOI":"10.1074\/jbc.M113.502328","volume":"289","author":"JC Rudell","year":"2014","unstructured":"Rudell JC, Borges LS, Rudell JB et al (2014) Determinants in the \u03b2 and \u03b4 subunit cytoplasmic loop regulate Golgi trafficking and surface expression of the muscle acetylcholine receptor. J Biol Chem 289:203\u2013214. https:\/\/doi.org\/10.1074\/jbc.M113.502328","journal-title":"J Biol Chem"},{"key":"5032_CR15","doi-asserted-by":"publisher","first-page":"1013","DOI":"10.1007\/s12192-023-01395-0","volume":"28","author":"S Brockm\u00f6ller","year":"2023","unstructured":"Brockm\u00f6ller S, Seeger T, Worek F et al (2023) Recombinant cellular model system for human muscle-type nicotinic acetylcholine receptor \u03b112\u03b21\u03b4\u03b5. Cell Stress Chaperones 28:1013\u20131025. https:\/\/doi.org\/10.1007\/s12192-023-01395-0","journal-title":"Cell Stress Chaperones"},{"key":"5032_CR16","doi-asserted-by":"publisher","first-page":"1558","DOI":"10.1038\/bjp.2008.185","volume":"154","author":"I Wessler","year":"2008","unstructured":"Wessler I, Kirkpatrick CJ (2008) Acetylcholine beyond neurons: the non-neuronal cholinergic system in humans. Br J Pharmacol 154:1558\u20131571. https:\/\/doi.org\/10.1038\/bjp.2008.185","journal-title":"Br J Pharmacol"},{"key":"5032_CR17","doi-asserted-by":"publisher","first-page":"1231","DOI":"10.1016\/0896-6273(95)90004-7","volume":"15","author":"A Karlin","year":"1995","unstructured":"Karlin A, Akabas MH (1995) Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins. Neuron 15:1231\u20131244. https:\/\/doi.org\/10.1016\/0896-6273(95)90004-7","journal-title":"Neuron"},{"key":"5032_CR18","doi-asserted-by":"publisher","DOI":"10.4061\/2011\/740583","volume":"2011","author":"S Suzuki","year":"2011","unstructured":"Suzuki S, Utsugisawa K, Nagane Y et al (2011) Three types of striational antibodies in myasthenia gravis. Autoimmune Dis 2011:740583. https:\/\/doi.org\/10.4061\/2011\/740583","journal-title":"Autoimmune Dis"},{"key":"5032_CR19","doi-asserted-by":"publisher","first-page":"1543","DOI":"10.1016\/B978-0-12-374367-1.00072-0","volume-title":"Hayes\u2019 handbook of pesticide toxicology","author":"M Lotti","year":"2010","unstructured":"Lotti M (2010) Clinical toxicology of anticholinesterase agents in humans. Hayes\u2019 handbook of pesticide toxicology. Academic Press, pp 1543\u20131589"},{"key":"5032_CR20","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.cca.2005.10.008","volume":"366","author":"LG Costa","year":"2006","unstructured":"Costa LG (2006) Current issues in organophosphate toxicology. Clin Chim Acta 366:1\u201313. https:\/\/doi.org\/10.1016\/j.cca.2005.10.008","journal-title":"Clin Chim Acta"},{"key":"5032_CR21","doi-asserted-by":"publisher","first-page":"146","DOI":"10.3109\/1040841X.2013.763222","volume":"40","author":"B Singh","year":"2014","unstructured":"Singh B, Kaur J, Singh K (2014) Microbial degradation of an organophosphate pesticide, malathion. Crit Rev Microbiol 40:146\u2013154. https:\/\/doi.org\/10.3109\/1040841X.2013.763222","journal-title":"Crit Rev Microbiol"},{"key":"5032_CR22","doi-asserted-by":"publisher","first-page":"462","DOI":"10.1007\/s10049-002-0462-0","volume":"5","author":"T Bey","year":"2002","unstructured":"Bey T, Walter FG (2002) Sarin, Soman, Tabun und VX. Notfall & Rettungsmedizin 5:462\u2013468. https:\/\/doi.org\/10.1007\/s10049-002-0462-0","journal-title":"Notfall & Rettungsmedizin"},{"key":"5032_CR23","doi-asserted-by":"publisher","first-page":"45","DOI":"10.1007\/978-1-4471-5625-3_3","volume":"27","author":"CM Morris","year":"2014","unstructured":"Morris CM, Savy C, Judge SJ et al (2014) Acute toxicity of organophosphorus compounds. Basic clin toxicol organophosphorus compd 27:45\u201378. https:\/\/doi.org\/10.1007\/978-1-4471-5625-3_3","journal-title":"Basic clin toxicol organophosphorus compd"},{"key":"5032_CR24","doi-asserted-by":"publisher","first-page":"2186","DOI":"10.1021\/acschemneuro.9b00041","volume":"10","author":"ML Paz","year":"2019","unstructured":"Paz ML, Barrantes FJ (2019) Autoimmune attack of the neuromuscular junction in myasthenia gravis: nicotinic acetylcholine receptors and other targets. ACS Chem Neurosci 10:2186\u20132194. https:\/\/doi.org\/10.1021\/acschemneuro.9b00041","journal-title":"ACS Chem Neurosci"},{"key":"5032_CR25","doi-asserted-by":"publisher","first-page":"17819","DOI":"10.1074\/jbc.M900030200","volume":"284","author":"CJB daCosta","year":"2009","unstructured":"daCosta CJB, Baenziger JE (2009) A lipid-dependent uncoupled conformation of the acetylcholine receptor. J Biol Chem 284:17819\u201317825. https:\/\/doi.org\/10.1074\/jbc.M900030200","journal-title":"J Biol Chem"},{"key":"5032_CR26","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/s12551-012-0078-7","volume":"5","author":"JE Baenziger","year":"2013","unstructured":"Baenziger JE, daCosta CJB (2013) Molecular mechanisms of acetylcholine receptor-lipid interactions: from model membranes to human biology. Biophys Rev 5:1\u20139. https:\/\/doi.org\/10.1007\/s12551-012-0078-7","journal-title":"Biophys Rev"},{"key":"5032_CR27","doi-asserted-by":"publisher","first-page":"20170174","DOI":"10.1098\/rstb.2017.0174","volume":"373","author":"J-P Changeux","year":"2018","unstructured":"Changeux J-P (2018) The nicotinic acetylcholine receptor: a typical \u201callosteric machine.\u201d Philos Trans R Soc Lond B Biol Sci 373:20170174. https:\/\/doi.org\/10.1098\/rstb.2017.0174","journal-title":"Philos Trans R Soc Lond B Biol Sci"},{"key":"5032_CR28","doi-asserted-by":"publisher","DOI":"10.1016\/j.neuropharm.2020.108086","volume":"171","author":"A Gharpure","year":"2020","unstructured":"Gharpure A, Noviello CM, Hibbs RE (2020) Progress in nicotinic receptor structural biology. Neuropharmacology 171:108086. https:\/\/doi.org\/10.1016\/j.neuropharm.2020.108086","journal-title":"Neuropharmacology"},{"key":"5032_CR29","doi-asserted-by":"publisher","first-page":"5753","DOI":"10.3390\/molecules26195753","volume":"26","author":"M Delgado-V\u00e9lez","year":"2021","unstructured":"Delgado-V\u00e9lez M, Quesada O, Villalobos-Santos JC et al (2021) Pursuing high-resolution structures of nicotinic acetylcholine receptors: lessons learned from five decades. Molecules 26:5753. https:\/\/doi.org\/10.3390\/molecules26195753","journal-title":"Molecules"},{"key":"5032_CR30","doi-asserted-by":"publisher","first-page":"5555","DOI":"10.1523\/JNEUROSCI.18-15-05555.1998","volume":"18","author":"WN Green","year":"1998","unstructured":"Green WN, Wanamaker CP (1998) Formation of the nicotinic acetylcholine receptor binding sites. J Neurosci 18:5555\u20135564","journal-title":"J Neurosci"},{"key":"5032_CR31","doi-asserted-by":"publisher","first-page":"22871","DOI":"10.1074\/jbc.271.37.22871","volume":"271","author":"SH Keller","year":"1996","unstructured":"Keller SH, Lindstrom J, Taylor P (1996) Involvement of the chaperone protein calnexin and the acetylcholine receptor \u03b2-subunit in the assembly and cell surface expression of the receptor. J Biol Chem 271:22871\u201322877","journal-title":"J Biol Chem"},{"key":"5032_CR32","doi-asserted-by":"publisher","first-page":"17064","DOI":"10.1074\/jbc.273.27.17064","volume":"273","author":"SH Keller","year":"1998","unstructured":"Keller SH, Lindstrom J, Taylor P (1998) Inhibition of glucose trimming with castanospermine reduces calnexin association and promotes proteasome degradation of the alpha-subunit of the nicotinic acetylcholine receptor. J Biol Chem 273:17064\u201317072. https:\/\/doi.org\/10.1074\/jbc.273.27.17064","journal-title":"J Biol Chem"},{"key":"5032_CR33","doi-asserted-by":"publisher","first-page":"171","DOI":"10.1085\/jgp.113.2.171","volume":"113","author":"SH Keller","year":"1999","unstructured":"Keller SH, Taylor P (1999) Determinants responsible for assembly of the nicotinic acetylcholine receptor. J Gen Physiol 113:171\u2013176","journal-title":"J Gen Physiol"},{"key":"5032_CR34","doi-asserted-by":"publisher","first-page":"5537","DOI":"10.1021\/acs.chemrev.8b00532","volume":"119","author":"JT Marinko","year":"2019","unstructured":"Marinko JT, Huang H, Penn WD et al (2019) Folding and misfolding of human membrane proteins in health and disease: from single molecules to cellular proteostasis. Chem Rev 119:5537\u20135606. https:\/\/doi.org\/10.1021\/acs.chemrev.8b00532","journal-title":"Chem Rev"},{"key":"5032_CR35","doi-asserted-by":"publisher","first-page":"1532","DOI":"10.1091\/mbc.E14-12-1615","volume":"26","author":"J Merulla","year":"2015","unstructured":"Merulla J, Sold\u00e0 T, Molinari M (2015) A novel UGGT1 and p97-dependent checkpoint for native ectodomains with ionizable intramembrane residue. Mol Biol Cell 26:1532\u20131542","journal-title":"Mol Biol Cell"},{"key":"5032_CR36","doi-asserted-by":"publisher","first-page":"231","DOI":"10.4052\/tigg.18.231","volume":"18","author":"Y Kamiya","year":"2006","unstructured":"Kamiya Y, Kato K (2006) Sugar recognition by intracellular lectins that determine the fates of glycoproteins. Trends Glycosci Glycotechnol 18:231\u2013244","journal-title":"Trends Glycosci Glycotechnol"},{"key":"5032_CR37","doi-asserted-by":"publisher","first-page":"31113","DOI":"10.1074\/jbc.M705369200","volume":"282","author":"CP Wanamaker","year":"2007","unstructured":"Wanamaker CP, Green WN (2007) Endoplasmic reticulum chaperones stabilize nicotinic receptor subunits and regulate receptor assembly. J Biol Chem 282:31113\u201331123. https:\/\/doi.org\/10.1074\/jbc.M705369200","journal-title":"J Biol Chem"},{"key":"5032_CR38","doi-asserted-by":"publisher","first-page":"2573","DOI":"10.1091\/mbc.10.8.2573","volume":"10","author":"JD Oliver","year":"1999","unstructured":"Oliver JD, Roderick HL, Llewellyn DH et al (1999) ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin. Mol Biol Cell 10:2573\u20132582","journal-title":"Mol Biol Cell"},{"key":"5032_CR39","doi-asserted-by":"publisher","first-page":"587","DOI":"10.1016\/S0959-440X(98)80148-6","volume":"8","author":"ES Trombetta","year":"1998","unstructured":"Trombetta ES, Helenius A (1998) Lectins as chaperones in glycoprotein folding. Curr Opin Struct Biol 8:587\u2013592","journal-title":"Curr Opin Struct Biol"},{"key":"5032_CR40","doi-asserted-by":"publisher","first-page":"1882","DOI":"10.1126\/science.286.5446.1882","volume":"286","author":"L Ellgaard","year":"1999","unstructured":"Ellgaard L, Molinari M, Helenius A (1999) Setting the standards: quality control in the secretory pathway. Science 286:1882\u20131888","journal-title":"Science"},{"key":"5032_CR41","doi-asserted-by":"publisher","first-page":"223","DOI":"10.1385\/CBB:39:3:223","volume":"39","author":"L Ellgaard","year":"2003","unstructured":"Ellgaard L, Frickel EM (2003) Calnexin, calreticulin, and ERp57: teammates in glycoprotein folding. Cell Biochem Biophys 39:223\u2013247","journal-title":"Cell Biochem Biophys"},{"key":"5032_CR42","doi-asserted-by":"publisher","first-page":"4156","DOI":"10.1038\/sj.emboj.7600436","volume":"23","author":"JC Christianson","year":"2004","unstructured":"Christianson JC, Green WN (2004) Regulation of nicotinic receptor expression by the ubiquitin\u2013proteasome system. EMBO J 23:4156\u20134165","journal-title":"EMBO J"},{"key":"5032_CR43","first-page":"507","volume":"10","author":"JL Brodsky","year":"1999","unstructured":"Brodsky JL, McCracken AA (1999) ER protein quality control and proteasome-mediated protein degradation. In seminars in cell & developmental biology. Academic Press 10:507\u2013513","journal-title":"Academic Press"},{"key":"5032_CR44","doi-asserted-by":"publisher","first-page":"33800","DOI":"10.1074\/jbc.M501813200","volume":"280","author":"CP Wanamaker","year":"2005","unstructured":"Wanamaker CP, Green WN (2005) N-linked glycosylation is required for nicotinic receptor assembly but not for subunit associations with calnexin. J Biol Chem 280:33800\u201333810. https:\/\/doi.org\/10.1074\/jbc.M501813200","journal-title":"J Biol Chem"},{"key":"5032_CR45","doi-asserted-by":"publisher","first-page":"219","DOI":"10.1016\/S0169-328X(96)00256-2","volume":"45","author":"VM Gehle","year":"1997","unstructured":"Gehle VM, Walcott EC, Nishizaki T et al (1997) N-glycosylation at the conserved sites ensures the expression of properly folded functional ACh receptors. Mol Brain Res 45:219\u2013229","journal-title":"Mol Brain Res"},{"key":"5032_CR46","doi-asserted-by":"publisher","first-page":"3000","DOI":"10.1523\/JNEUROSCI.21-09-03000.2001","volume":"21","author":"M Mitra","year":"2001","unstructured":"Mitra M, Wanamaker CP, Green WN (2001) Rearrangement of nicotinic receptor \u03b1 subunits during formation of the ligand binding sites. J Neurosci 21:3000\u20133008","journal-title":"J Neurosci"},{"key":"5032_CR47","doi-asserted-by":"publisher","first-page":"30873","DOI":"10.1074\/jbc.272.49.30873","volume":"272","author":"JP Li\u00e8vremont","year":"1997","unstructured":"Li\u00e8vremont JP, Rizzuto R, Hendershot L et al (1997) BiP, a major chaperone protein of the endoplasmic reticulum lumen, plays a direct and important role in the storage of the rapidly exchanging pool of Ca2+. J Biol Chem 272:30873\u201330879. https:\/\/doi.org\/10.1074\/jbc.272.49.30873","journal-title":"J Biol Chem"},{"key":"5032_CR48","doi-asserted-by":"publisher","first-page":"841","DOI":"10.1083\/jcb.117.4.841","volume":"117","author":"JR Forsayeth","year":"1992","unstructured":"Forsayeth JR, Gu Y, Hall ZW (1992) BiP forms stable complexes with unassembled subunits of the acetylcholine receptor in transfected COS cells and in C2 muscle cells. J Cell Biol 117:841\u2013847","journal-title":"J Cell Biol"},{"key":"5032_CR49","doi-asserted-by":"publisher","first-page":"1125","DOI":"10.1083\/jcb.113.5.1125","volume":"113","author":"P Blount","year":"1991","unstructured":"Blount P, Merlie JP (1991) BIP associates with newly synthesized subunits of the mouse muscle nicotinic receptor. J Cell Biol 113:1125\u20131132. https:\/\/doi.org\/10.1083\/jcb.113.5.1125","journal-title":"J Cell Biol"},{"key":"5032_CR50","doi-asserted-by":"publisher","first-page":"14","DOI":"10.1016\/j.gene.2017.03.005","volume":"618","author":"J Wang","year":"2017","unstructured":"Wang J, Lee J, Liem D et al (2017) HSPA5 Gene encoding Hsp70 chaperone BiP in the endoplasmic reticulum. Gene 618:14\u201323. https:\/\/doi.org\/10.1016\/j.gene.2017.03.005","journal-title":"Gene"},{"key":"5032_CR51","doi-asserted-by":"publisher","first-page":"10345","DOI":"10.1073\/pnas.91.22.10345","volume":"91","author":"A Szabo","year":"1994","unstructured":"Szabo A, Langer T, Schr\u00f6der H et al (1994) The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE. Proc Natl Acad Sci 91:10345\u201310349","journal-title":"Proc Natl Acad Sci"},{"key":"5032_CR52","doi-asserted-by":"publisher","first-page":"163","DOI":"10.1085\/jgp.113.2.163","volume":"113","author":"WN Green","year":"1999","unstructured":"Green WN (1999) Ion channel assembly: creating structures that function. J Gen Physiol 113:163\u2013170","journal-title":"J Gen Physiol"},{"key":"5032_CR53","doi-asserted-by":"publisher","first-page":"20513","DOI":"10.1074\/jbc.274.29.20513","volume":"274","author":"VK Ramanathan","year":"1999","unstructured":"Ramanathan VK, Hall ZW (1999) Altered glycosylation sites of the delta subunit of the acetylcholine receptor (AChR) reduce alpha delta association and receptor assembly. J Biol Chem 274:20513\u201320520. https:\/\/doi.org\/10.1074\/jbc.274.29.20513","journal-title":"J Biol Chem"},{"key":"5032_CR54","doi-asserted-by":"publisher","first-page":"751","DOI":"10.1016\/1074-5521(95)90103-5","volume":"2","author":"KW Rickert","year":"1995","unstructured":"Rickert KW, Imperiali B (1995) Analysis of the conserved glycosylation site in the nicotinic acetylcholine receptor: potential roles in complex assembly. Chem Biol 2:751\u2013759","journal-title":"Chem Biol"},{"key":"5032_CR55","doi-asserted-by":"publisher","first-page":"20945","DOI":"10.1074\/jbc.272.33.20945","volume":"272","author":"WN Green","year":"1997","unstructured":"Green WN, Wanamaker CP (1997) The role of the cystine loop in acetylcholine receptor assembly. J Biol Chem 272:20945\u201320953. https:\/\/doi.org\/10.1074\/jbc.272.33.20945","journal-title":"J Biol Chem"},{"key":"5032_CR56","doi-asserted-by":"publisher","first-page":"53","DOI":"10.1111\/j.1749-6632.1986.tb21503.x","volume":"463","author":"A Karlin","year":"1986","unstructured":"Karlin A, Cox RN, Dipaola M et al (1986) Functional domains of the nicotinic acetylcholine receptor. Ann N Y Acad Sci 463:53\u201369","journal-title":"Ann N Y Acad Sci"},{"key":"5032_CR57","doi-asserted-by":"publisher","first-page":"2613","DOI":"10.1083\/jcb.111.6.2613","volume":"111","author":"P Blount","year":"1990","unstructured":"Blount P, Merlie JP (1990) Mutational analysis of muscle nicotinic acetylcholine receptor subunit assembly. J Cell Biol 111:2613\u20132622","journal-title":"J Cell Biol"},{"key":"5032_CR58","doi-asserted-by":"publisher","first-page":"747","DOI":"10.1016\/0092-8674(83)90531-7","volume":"34","author":"JP Merlie","year":"1983","unstructured":"Merlie JP, Lindstrom J (1983) Assembly in vivo of mouse muscle acetylcholine receptor: identification of an \u03b1 subunit species that may be an assembly intermediate. Cell 34:747\u2013757","journal-title":"Cell"},{"key":"5032_CR59","doi-asserted-by":"publisher","first-page":"472","DOI":"10.1016\/j.semcdb.2009.12.008","volume":"21","author":"JH Otero","year":"2010","unstructured":"Otero JH, Liz\u00e1k B, Hendershot LM (2010) Life and death of a BiP substrate. Semin Cell Dev Biol 21:472\u2013478. https:\/\/doi.org\/10.1016\/j.semcdb.2009.12.008","journal-title":"Semin Cell Dev Biol"},{"key":"5032_CR60","doi-asserted-by":"publisher","first-page":"227","DOI":"10.1042\/EBC20160003","volume":"60","author":"K McCaffrey","year":"2016","unstructured":"McCaffrey K, Braakman I (2016) Protein quality control at the endoplasmic reticulum. Essays Biochem 60:227\u2013235. https:\/\/doi.org\/10.1042\/EBC20160003","journal-title":"Essays Biochem"},{"key":"5032_CR61","doi-asserted-by":"publisher","first-page":"1589","DOI":"10.1016\/j.jmb.2015.02.011","volume":"427","author":"J Behnke","year":"2015","unstructured":"Behnke J, Feige MJ, Hendershot LM (2015) BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions. J Mol Biol 427:1589\u20131608. https:\/\/doi.org\/10.1016\/j.jmb.2015.02.011","journal-title":"J Mol Biol"},{"key":"5032_CR62","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1007\/978-3-319-11731-7_9","volume":"78","author":"A Melnyk","year":"2015","unstructured":"Melnyk A, Rieger H, Zimmermann R (2015) Co-chaperones of the mammalian endoplasmic reticulum. Subcell Biochem 78:179\u2013200. https:\/\/doi.org\/10.1007\/978-3-319-11731-7_9","journal-title":"Subcell Biochem"},{"key":"5032_CR63","doi-asserted-by":"publisher","first-page":"89","DOI":"10.1038\/nrm3270","volume":"13","author":"C Hetz","year":"2012","unstructured":"Hetz C (2012) The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat Rev Mol Cell Biol 13:89\u2013102. https:\/\/doi.org\/10.1038\/nrm3270","journal-title":"Nat Rev Mol Cell Biol"},{"key":"5032_CR64","doi-asserted-by":"publisher","first-page":"122","DOI":"10.1016\/S0014-5793(02)02289-5","volume":"514","author":"RV Rao","year":"2002","unstructured":"Rao RV, Peel A, Logvinova A et al (2002) Coupling endoplasmic reticulum stress to the cell death program: role of the ER chaperone GRP78. FEBS Lett 514:122\u2013128","journal-title":"FEBS Lett"},{"key":"5032_CR65","doi-asserted-by":"publisher","first-page":"20915","DOI":"10.1074\/jbc.M212328200","volume":"278","author":"RK Reddy","year":"2003","unstructured":"Reddy RK, Mao C, Baumeister P et al (2003) Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors: role of ATP binding site in suppression of caspase-7 activation. J Biol Chem 278:20915\u201320924. https:\/\/doi.org\/10.1074\/jbc.M212328200","journal-title":"J Biol Chem"},{"key":"5032_CR66","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.03496.001","volume":"3","author":"J Wang","year":"2014","unstructured":"Wang J, Pareja KA, Kaiser CA et al (2014) Redox signaling via the molecular chaperone BiP protects cells against endoplasmic reticulum-derived oxidative stress. Elife 3:e03496. https:\/\/doi.org\/10.7554\/eLife.03496.001","journal-title":"Elife"},{"key":"5032_CR67","doi-asserted-by":"publisher","first-page":"963","DOI":"10.1038\/nn918","volume":"5","author":"JM Wang","year":"2002","unstructured":"Wang JM, Zhang L, Yao Y et al (2002) A transmembrane motif governs the surface trafficking of nicotinic acetylcholine receptors. Nat Neurosci 5:963\u2013970. https:\/\/doi.org\/10.1038\/nn918","journal-title":"Nat Neurosci"},{"key":"5032_CR68","doi-asserted-by":"publisher","first-page":"915","DOI":"10.1083\/jcb.200208074","volume":"159","author":"P Malkus","year":"2002","unstructured":"Malkus P, Jiang F, Schekman R (2002) Concentrative sorting of secretory cargo proteins into COPII-coated vesicles. J Cell Biol 159:915\u2013921. https:\/\/doi.org\/10.1083\/jcb.200208074","journal-title":"J Cell Biol"},{"key":"5032_CR69","doi-asserted-by":"publisher","first-page":"2043","DOI":"10.1038\/emboj.2008.136","volume":"27","author":"H Farhan","year":"2008","unstructured":"Farhan H, Weiss M, Tani K et al (2008) Adaptation of endoplasmic reticulum exit sites to acute and chronic increases in cargo load. The EMBO journal, 27(15), 2043\u20132054. EMBO J 27:2043\u20132054","journal-title":"EMBO J"},{"key":"5032_CR70","doi-asserted-by":"publisher","first-page":"997","DOI":"10.1083\/jcb.200912082","volume":"189","author":"H Farhan","year":"2010","unstructured":"Farhan H, Wendeler MW, Mitrovic S et al (2010) MAPK signaling to the early secretory pathway revealed by kinase\/phosphatase functional screening. J Cell Biol 189:997\u20131011. https:\/\/doi.org\/10.1083\/jcb.200912082","journal-title":"J Cell Biol"},{"issue":"18","key":"5032_CR71","doi-asserted-by":"publisher","first-page":"e110596","DOI":"10.15252\/embj.2022110596","volume":"41","author":"S Phuyal","year":"2022","unstructured":"Phuyal S, Djaerff E, Le Roux AL et al (2022) Mechanical strain stimulates COPII-dependent secretory trafficking via Rac1. EMBO J 41(18):e110596. https:\/\/doi.org\/10.15252\/embj.2022110596","journal-title":"EMBO J"},{"key":"5032_CR72","doi-asserted-by":"publisher","first-page":"157","DOI":"10.3389\/fcell.2019.00157","volume":"7","author":"P Fisher","year":"2019","unstructured":"Fisher P, Thomas-Oates J, Wood AJ et al (2019) The N-Glycosylation processing potential of the mammalian Golgi apparatus. Front Cell Dev Biol 7:157. https:\/\/doi.org\/10.3389\/fcell.2019.00157","journal-title":"Front Cell Dev Biol"},{"key":"5032_CR73","doi-asserted-by":"publisher","first-page":"303","DOI":"10.1111\/j.1600-0854.2009.01026.x","volume":"11","author":"C Russell","year":"2010","unstructured":"Russell C, Stagg SM (2010) New insights into the structural mechanisms of the COPII coat. Traffic 11:303\u2013310. https:\/\/doi.org\/10.1111\/j.1600-0854.2009.01026.x","journal-title":"Traffic"},{"key":"5032_CR74","doi-asserted-by":"publisher","first-page":"377","DOI":"10.1038\/ncb1371","volume":"8","author":"D Zeuschner","year":"2006","unstructured":"Zeuschner D, Geerts WJC, van Donselaar E et al (2006) Immuno-electron tomography of ER exit sites reveals the existence of free COPII-coated transport carriers. Nat Cell Biol 8:377\u2013383. https:\/\/doi.org\/10.1038\/ncb1371","journal-title":"Nat Cell Biol"},{"key":"5032_CR75","doi-asserted-by":"publisher","first-page":"1731","DOI":"10.1083\/jcb.201703084","volume":"216","author":"M Maeda","year":"2017","unstructured":"Maeda M, Katada T, Saito K (2017) TANGO1 recruits Sec16 to coordinately organize ER exit sites for efficient secretion. J Cell Biol 216:1731\u20131743. https:\/\/doi.org\/10.1083\/jcb.201703084","journal-title":"J Cell Biol"},{"key":"5032_CR76","doi-asserted-by":"publisher","first-page":"2008","DOI":"10.1091\/mbc.E16-03-0180","volume":"27","author":"T Tanabe","year":"2016","unstructured":"Tanabe T, Maeda M, Saito K et al (2016) Dual function of cTAGE5 in collagen export from the endoplasmic reticulum. Mol Biol Cell 27:2008\u20132013","journal-title":"Mol Biol Cell"},{"key":"5032_CR77","doi-asserted-by":"publisher","first-page":"528","DOI":"10.1016\/j.ceb.2010.05.008","volume":"22","author":"VW Hsu","year":"2010","unstructured":"Hsu VW, Prekeris R (2010) Transport at the recycling endosome. Curr Opin Cell Biol 22:528\u2013534. https:\/\/doi.org\/10.1016\/j.ceb.2010.05.008","journal-title":"Curr Opin Cell Biol"},{"key":"5032_CR78","doi-asserted-by":"publisher","first-page":"31","DOI":"10.1182\/blood-2012-01-292086","volume":"120","author":"R Khoriaty","year":"2012","unstructured":"Khoriaty R, Vasievich MP, Ginsburg D (2012) The COPII pathway and hematologic disease. Blood 120:31\u201338. https:\/\/doi.org\/10.1182\/blood-2012-01-292086","journal-title":"Blood"},{"key":"5032_CR79","doi-asserted-by":"publisher","first-page":"891","DOI":"10.1016\/j.cell.2008.12.025","volume":"136","author":"K Saito","year":"2009","unstructured":"Saito K, Chen M, Bard F et al (2009) TANGO1 facilitates cargo loading at endoplasmic reticulum exit sites. Cell 136:891\u2013902. https:\/\/doi.org\/10.1016\/j.cell.2008.12.025","journal-title":"Cell"},{"key":"5032_CR80","doi-asserted-by":"publisher","first-page":"497","DOI":"10.1016\/s0092-8674(03)00609-3","volume":"114","author":"EA Miller","year":"2003","unstructured":"Miller EA, Beilharz TH, Malkus PN et al (2003) Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell 114:497\u2013509. https:\/\/doi.org\/10.1016\/s0092-8674(03)00609-3","journal-title":"Cell"},{"key":"5032_CR81","doi-asserted-by":"publisher","first-page":"258","DOI":"10.1038\/sj.embor.7400893","volume":"8","author":"MW Wendeler","year":"2007","unstructured":"Wendeler MW, Paccaud JP, Hauri HP (2007) Role of Sec24 isoforms in selective export of membrane proteins from the endoplasmic reticulum. EMBO Rep 8:258\u2013264. https:\/\/doi.org\/10.1038\/sj.embor.7400893","journal-title":"EMBO Rep"},{"key":"5032_CR82","doi-asserted-by":"publisher","first-page":"10061","DOI":"10.1073\/pnas.1605916113","volume":"113","author":"W Ma","year":"2016","unstructured":"Ma W, Goldberg J (2016) TANGO1\/cTAGE5 receptor as a polyvalent template for assembly of large COPII coats. Proc Natl Acad Sci U S A 113:10061\u201310066. https:\/\/doi.org\/10.1073\/pnas.1605916113","journal-title":"Proc Natl Acad Sci U S A"},{"key":"5032_CR83","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.32723.001","volume":"7","author":"I Raote","year":"2018","unstructured":"Raote I, Ortega-Bellido M, Santos AJ et al (2018) TANGO1 builds a machine for collagen export by recruiting and spatially organizing COPII, tethers and membranes. Elife 7:e32723. https:\/\/doi.org\/10.7554\/eLife.32723.001","journal-title":"Elife"},{"key":"5032_CR84","doi-asserted-by":"publisher","first-page":"50","DOI":"10.1016\/j.ceb.2018.04.009","volume":"54","author":"A Payapilly","year":"2018","unstructured":"Payapilly A, Malliri A (2018) Compartmentalisation of RAC1 signalling. Curr Opin Cell Biol 54:50\u201356. https:\/\/doi.org\/10.1016\/j.ceb.2018.04.009","journal-title":"Curr Opin Cell Biol"},{"key":"5032_CR85","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.202104062","volume":"220","author":"S Phuyal","year":"2021","unstructured":"Phuyal S, Farhan H (2021) Want to leave the ER? We offer vesicles, tubules, and tunnels. J Cell Biol 220:e202104062","journal-title":"J Cell Biol"},{"key":"5032_CR86","doi-asserted-by":"publisher","first-page":"997","DOI":"10.1083\/jcb.200408135","volume":"167","author":"D Xu","year":"2004","unstructured":"Xu D, Hay JC (2004) Reconstitution of COPII vesicle fusion to generate a pre-Golgi intermediate compartment. J Cell Biol 167:997\u20131003. https:\/\/doi.org\/10.1083\/jcb.200408135","journal-title":"J Cell Biol"},{"key":"5032_CR87","doi-asserted-by":"publisher","first-page":"737","DOI":"10.1083\/jcb.201811073","volume":"218","author":"I Raote","year":"2019","unstructured":"Raote I, Malhotra V (2019) Protein transport by vesicles and tunnels. J Cell Biol 218:737\u2013739. https:\/\/doi.org\/10.1083\/jcb.201811073","journal-title":"J Cell Biol"},{"key":"5032_CR88","doi-asserted-by":"publisher","first-page":"587","DOI":"10.1242\/jcs.113.4.587","volume":"113","author":"HP Hauri","year":"2000","unstructured":"Hauri HP, Kappeler F, Andersson H et al (2000) ERGIC-53 and traffic in the secretory pathway. J Cell Sci 113:587\u2013596","journal-title":"J Cell Sci"},{"key":"5032_CR89","doi-asserted-by":"publisher","first-page":"20","DOI":"10.1038\/ncb2390","volume":"14","author":"G Zanetti","year":"2011","unstructured":"Zanetti G, Pahuja KB, Studer S et al (2011) COPII and the regulation of protein sorting in mammals. Nat Cell Biol 14:20\u201328. https:\/\/doi.org\/10.1038\/ncb2390","journal-title":"Nat Cell Biol"},{"key":"5032_CR90","doi-asserted-by":"publisher","first-page":"1857","DOI":"10.1074\/jbc.M709384200","volume":"283","author":"Y Kamiya","year":"2008","unstructured":"Kamiya Y, Kamiya D, Yamamoto K et al (2008) Molecular basis of sugar recognition by the human L-type lectins ERGIC-53, VIPL, and VIP36. J Biol Chem 283:1857\u20131861. https:\/\/doi.org\/10.1074\/jbc.M709384200","journal-title":"J Biol Chem"},{"key":"5032_CR91","doi-asserted-by":"publisher","first-page":"651","DOI":"10.1111\/j.1600-0854.2010.01043.x","volume":"11","author":"M Cortini","year":"2010","unstructured":"Cortini M, Sitia R (2010) ERp44 and ERGIC-53 synergize in coupling efficiency and fidelity of IgM polymerization and secretion. Traffic 11:651\u2013659. https:\/\/doi.org\/10.1111\/j.1600-0854.2010.01043.x","journal-title":"Traffic"},{"key":"5032_CR92","doi-asserted-by":"publisher","DOI":"10.1016\/j.isci.2021.102244","volume":"24","author":"T Tempio","year":"2021","unstructured":"Tempio T, Orsi A, Sicari D et al (2021) A virtuous cycle operated by ERp44 and ERGIC-53 guarantees proteostasis in the early secretory compartment. IScience 24:102244","journal-title":"IScience"},{"key":"5032_CR93","doi-asserted-by":"publisher","first-page":"356","DOI":"10.1016\/j.bbrc.2019.02.053","volume":"511","author":"YL Fu","year":"2019","unstructured":"Fu YL, Zhang B, Mu TW (2019) LMAN1 (ERGIC-53) promotes trafficking of neuroreceptors. Biochem Biophys Res Commun 511:356\u2013362. https:\/\/doi.org\/10.1016\/j.bbrc.2019.02.053","journal-title":"Biochem Biophys Res Commun"},{"key":"5032_CR94","doi-asserted-by":"publisher","first-page":"15080","DOI":"10.1074\/jbc.274.21.15080","volume":"274","author":"H Andersson","year":"1999","unstructured":"Andersson H, Kappeler F, Hauri HP (1999) Protein targeting to endoplasmic reticulum by dilysine signals involves direct retention in addition to retrieval. J Biol Chem 274:15080\u201315084. https:\/\/doi.org\/10.1074\/jbc.274.21.15080","journal-title":"J Biol Chem"},{"key":"5032_CR95","doi-asserted-by":"publisher","first-page":"883","DOI":"10.1083\/jcb.124.6.883","volume":"124","author":"S Hara-Kuge","year":"1994","unstructured":"Hara-Kuge S, Kuge O, Orci L et al (1994) En bloc incorporation of coatomer subunits during the assembly of COP-coated vesicles. J Cell Biol 124:883\u2013892","journal-title":"J Cell Biol"},{"key":"5032_CR96","doi-asserted-by":"publisher","first-page":"248","DOI":"10.1038\/349248a0","volume":"349","author":"MG Waters","year":"1991","unstructured":"Waters MG, Serafini T, Rothman JE (1991) \u201cCoatomer\u201d: a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles. Nature 349:248\u2013251","journal-title":"Nature"},{"key":"5032_CR97","doi-asserted-by":"publisher","first-page":"3905","DOI":"10.1093\/emboj\/19.15.3905","volume":"19","author":"A Eugster","year":"2000","unstructured":"Eugster A, Frigerio G, Dale M et al (2000) COP I domains required for coatomer integrity, and novel interactions with ARF and ARF-GAP. EMBO J 19:3905\u20133917","journal-title":"EMBO J"},{"key":"5032_CR98","doi-asserted-by":"publisher","first-page":"769","DOI":"10.1083\/jcb.201610031","volume":"215","author":"N Gomez-Navarro","year":"2016","unstructured":"Gomez-Navarro N, Miller E (2016) Protein sorting at the ER-Golgi interface. J Cell Biol 215:769\u2013778. https:\/\/doi.org\/10.1083\/jcb.201610031","journal-title":"J Cell Biol"},{"key":"5032_CR99","doi-asserted-by":"publisher","first-page":"1255","DOI":"10.1016\/j.devcel.2012.10.017","volume":"23","author":"LP Jackson","year":"2012","unstructured":"Jackson LP, Lewis M, Kent HM et al (2012) Molecular basis for recognition of dilysine trafficking motifs by COPI. Dev Cell 23:1255\u20131262. https:\/\/doi.org\/10.1016\/j.devcel.2012.10.017","journal-title":"Dev Cell"},{"key":"5032_CR100","doi-asserted-by":"publisher","first-page":"6408","DOI":"10.1073\/pnas.89.14.6408","volume":"89","author":"JG Donaldson","year":"1992","unstructured":"Donaldson JG, Cassel D, Kahn RA et al (1992) ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein beta-COP to Golgi membranes. Proc Natl Acad Sci 89:6408\u20136412","journal-title":"Proc Natl Acad Sci"},{"key":"5032_CR101","doi-asserted-by":"publisher","first-page":"350","DOI":"10.1038\/360350a0","volume":"360","author":"JG Donaldson","year":"1992","unstructured":"Donaldson JG, Finazzi D, Klausner RD (1992) Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein. Nature 360:350\u2013352","journal-title":"Nature"},{"key":"5032_CR102","doi-asserted-by":"publisher","first-page":"352","DOI":"10.1038\/360352a0","volume":"360","author":"JB Helms","year":"1992","unstructured":"Helms JB, Rothman JE (1992) Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF. Nature 360:352\u2013354","journal-title":"Nature"},{"key":"5032_CR103","doi-asserted-by":"publisher","first-page":"1365","DOI":"10.1083\/jcb.123.6.1365","volume":"123","author":"G Tanigawa","year":"1993","unstructured":"Tanigawa G, Orci L, Amherdt M et al (1993) Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles. J Cell Biol 123:1365\u20131371","journal-title":"J Cell Biol"},{"key":"5032_CR104","doi-asserted-by":"publisher","first-page":"3758","DOI":"10.1016\/j.febslet.2009.10.056","volume":"583","author":"VW Hsu","year":"2009","unstructured":"Hsu VW, Yang J-S (2009) Mechanisms of COPI vesicle formation. FEBS Lett 583:3758\u20133763. https:\/\/doi.org\/10.1016\/j.febslet.2009.10.056","journal-title":"FEBS Lett"},{"key":"5032_CR105","doi-asserted-by":"publisher","first-page":"1349","DOI":"10.1016\/0092-8674(90)90698-E","volume":"61","author":"JC Semenza","year":"1990","unstructured":"Semenza JC, Hardwick KG, Dean N et al (1990) ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway. Cell 61:1349\u20131357","journal-title":"Cell"},{"issue":"31","key":"5032_CR106","doi-asserted-by":"publisher","first-page":"10203","DOI":"10.1021\/bi960807x","volume":"35","author":"AA Scheel","year":"1996","unstructured":"Scheel AA, Pelham HR (1996) Purification and characterization of the human KDEL receptor. Biochemistry 35(31):10203\u201310209. https:\/\/doi.org\/10.1021\/bi960807x","journal-title":"Biochemistry"},{"key":"5032_CR107","doi-asserted-by":"publisher","first-page":"139","DOI":"10.1016\/S1534-5807(01)00004-1","volume":"1","author":"I Majoul","year":"2001","unstructured":"Majoul I, Straub M, Hell SW et al (2001) KDEL-cargo regulates interactions between proteins involved in COPI vesicle traffic: measurements in living cells using FRET. Dev Cell 1:139\u2013153","journal-title":"Dev Cell"},{"key":"5032_CR108","doi-asserted-by":"publisher","first-page":"621","DOI":"10.1073\/pnas.1001624108","volume":"108","author":"C Valkova","year":"2011","unstructured":"Valkova C, Albrizio M, R\u00f6der IV et al (2011) Sorting receptor Rer1 controls surface expression of muscle acetylcholine receptors by ER retention of unassembled alpha-subunits. Proc Natl Acad Sci U S A 108:621\u2013625. https:\/\/doi.org\/10.1073\/pnas.1001624108","journal-title":"Proc Natl Acad Sci U S A"},{"key":"5032_CR109","doi-asserted-by":"publisher","DOI":"10.1242\/jcs.231423","author":"W Annaert","year":"2020","unstructured":"Annaert W, Kaether C (2020) Bring it back, bring it back, don\u2019t take it away from me\u2014the sorting receptor RER1. J Cell Sci. https:\/\/doi.org\/10.1242\/jcs.231423","journal-title":"J Cell Sci"},{"key":"5032_CR110","doi-asserted-by":"publisher","first-page":"9693","DOI":"10.1073\/pnas.94.18.9693","volume":"94","author":"K Sato","year":"1997","unstructured":"Sato K, Sato M, Nakano A (1997) Rer1p as common machinery for the endoplasmic reticulum localization of membrane proteins. Proc Natl Acad Sci 94:9693\u20139698","journal-title":"Proc Natl Acad Sci"},{"key":"5032_CR111","doi-asserted-by":"publisher","first-page":"3605","DOI":"10.1091\/mbc.e02-12-0777","volume":"14","author":"K Sato","year":"2003","unstructured":"Sato K, Sato M, Nakano A (2003) Rer1p, a retrieval receptor for ER membrane proteins, recognizes transmembrane domains in multiple modes. Mol Biol Cell 14:3605\u20133616. https:\/\/doi.org\/10.1091\/mbc.e02-12-0777","journal-title":"Mol Biol Cell"},{"key":"5032_CR112","doi-asserted-by":"publisher","first-page":"3183","DOI":"10.1016\/j.jmb.2016.02.030","volume":"428","author":"X Zhang","year":"2016","unstructured":"Zhang X, Wang Y (2016) Glycosylation quality control by the Golgi structure. J Mol Biol 428:3183\u20133193. https:\/\/doi.org\/10.1016\/j.jmb.2016.02.030","journal-title":"J Mol Biol"},{"key":"5032_CR113","doi-asserted-by":"publisher","DOI":"10.1101\/cshperspect.a005199","author":"P Stanley","year":"2011","unstructured":"Stanley P (2011) Golgi glycosylation. Cold Spring Harb Perspect Biol. https:\/\/doi.org\/10.1101\/cshperspect.a005199","journal-title":"Cold Spring Harb Perspect Biol"},{"key":"5032_CR114","doi-asserted-by":"publisher","first-page":"2470","DOI":"10.1083\/jcb.201903068","volume":"218","author":"FG Centonze","year":"2019","unstructured":"Centonze FG, Reiterer V, Nalbach K et al (2019) LTK is an ER-resident receptor tyrosine kinase that regulates secretion. J Cell Biol 218:2470\u20132480. https:\/\/doi.org\/10.1083\/jcb.201903068","journal-title":"J Cell Biol"},{"key":"5032_CR115","volume-title":"Essentials of glycobiology: N-glycans","author":"P Stanley","year":"2015","unstructured":"Stanley P, Taniguchi N, Aebi M (2015) Essentials of glycobiology: N-glycans. Cold Spring Harbor, New York"},{"key":"5032_CR116","doi-asserted-by":"publisher","first-page":"5759","DOI":"10.1074\/jbc.M109.068353","volume":"285","author":"SJ North","year":"2010","unstructured":"North SJ, Huang HH, Sundaram S et al (2010) Glycomics profiling of Chinese hamster ovary cell glycosylation mutants reveals N-glycans of a novel size and complexity. J Biol Chem 285:5759\u20135775. https:\/\/doi.org\/10.1074\/jbc.M109.068353","journal-title":"J Biol Chem"},{"key":"5032_CR117","doi-asserted-by":"publisher","first-page":"271","DOI":"10.1007\/s00418-013-1117-6","volume":"140","author":"R Willett","year":"2013","unstructured":"Willett R, Ungar D, Lupashin V (2013) The Golgi puppet master: COG complex at center stage of membrane trafficking interactions. Histochem Cell Biol 140:271\u2013283. https:\/\/doi.org\/10.1007\/s00418-013-1117-6","journal-title":"Histochem Cell Biol"},{"key":"5032_CR118","doi-asserted-by":"publisher","first-page":"405","DOI":"10.1016\/s0955-0674(03)00054-1","volume":"15","author":"FA Barr","year":"2003","unstructured":"Barr FA, Short B (2003) Golgins in the structure and dynamics of the Golgi apparatus. Curr Opin Cell Biol 15:405\u2013413. https:\/\/doi.org\/10.1016\/s0955-0674(03)00054-1","journal-title":"Curr Opin Cell Biol"},{"key":"5032_CR119","doi-asserted-by":"publisher","first-page":"153","DOI":"10.1016\/S0092-8674(03)01079-1","volume":"116","author":"JS Bonifacino","year":"2004","unstructured":"Bonifacino JS, Glick BS (2004) The mechanisms of vesicle budding and fusion. Cell 116:153\u2013166","journal-title":"Cell"},{"key":"5032_CR120","doi-asserted-by":"publisher","first-page":"444","DOI":"10.1126\/science.289.5478.444","volume":"289","author":"BB Allan","year":"2000","unstructured":"Allan BB, Moyer BD, Balch WE (2000) Rab1 recruitment of p115 into a cis-SNARE complex: programming budding COPII vesicles for fusion. Science 289:444\u2013448","journal-title":"Science"},{"key":"5032_CR121","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1016\/S0092-8674(00)80407-9","volume":"91","author":"FA Barr","year":"1997","unstructured":"Barr FA, Puype M, Vandekerckhove J et al (1997) GRASP65, a protein involved in the stacking of Golgi cisternae. Cell 91:253\u2013262","journal-title":"Cell"},{"key":"5032_CR122","doi-asserted-by":"publisher","first-page":"445","DOI":"10.1016\/S0092-8674(00)80225-1","volume":"89","author":"N Nakamura","year":"1997","unstructured":"Nakamura N, Lowe M, Levine TP et al (1997) The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner. Cell 89:445\u2013455","journal-title":"Cell"},{"key":"5032_CR123","doi-asserted-by":"publisher","first-page":"268","DOI":"10.1034\/j.1600-0854.2001.1o007.x","volume":"2","author":"BD Moyer","year":"2001","unstructured":"Moyer BD, Allan BB, Balch WE (2001) Rab1 interaction with a GM130 effector complex regulates COPII vesicle cis\u2013Golgi tethering. Traffic 2:268\u2013276. https:\/\/doi.org\/10.1034\/j.1600-0854.2001.1o007.x","journal-title":"Traffic"},{"key":"5032_CR124","doi-asserted-by":"publisher","first-page":"336","DOI":"10.1093\/embo-reports\/kve065","volume":"2","author":"T Weide","year":"2001","unstructured":"Weide T, Bayer M, K\u00f6ster M et al (2001) The Golgi matrix protein GM130: a specific interacting partner of the small GTPase rab1b. EMBO Rep 2:336\u2013341. https:\/\/doi.org\/10.1093\/embo-reports\/kve065","journal-title":"EMBO Rep"},{"key":"5032_CR125","doi-asserted-by":"publisher","first-page":"4229","DOI":"10.1074\/jbc.M112.426767","volume":"288","author":"VJ Miller","year":"2013","unstructured":"Miller VJ, Sharma P, Kudlyk TA et al (2013) Molecular insights into vesicle tethering at the Golgi by the conserved oligomeric Golgi (COG) complex and the golgin TATA element modulatory factor (TMF). J Biol Chem 288:4229\u20134240. https:\/\/doi.org\/10.1074\/jbc.M112.426767","journal-title":"J Biol Chem"},{"key":"5032_CR126","doi-asserted-by":"publisher","first-page":"542","DOI":"10.3109\/07853890.2011.579150","volume":"44","author":"A Rivinoja","year":"2012","unstructured":"Rivinoja A, Pujol FM, Hassinen A et al (2012) Golgi pH, its regulation and roles in human disease. Ann Med 44:542\u2013554. https:\/\/doi.org\/10.3109\/07853890.2011.579150","journal-title":"Ann Med"},{"key":"5032_CR127","doi-asserted-by":"publisher","DOI":"10.1101\/cshperspect.a007849","volume":"3","author":"MJ Klute","year":"2011","unstructured":"Klute MJ, Melan\u00e7on P, Dacks JB (2011) Evolution and diversity of the Golgi. Cold Spring Harb Perspect Biol 3:a007849. https:\/\/doi.org\/10.1101\/cshperspect.a007849","journal-title":"Cold Spring Harb Perspect Biol"},{"key":"5032_CR128","doi-asserted-by":"publisher","first-page":"1659","DOI":"10.1038\/ncomms2669","volume":"4","author":"Y Xiang","year":"2013","unstructured":"Xiang Y, Zhang X, Nix DB et al (2013) Regulation of protein glycosylation and sorting by the Golgi matrix proteins GRASP55\/65. Nat Commun 4:1659. https:\/\/doi.org\/10.1038\/ncomms2669","journal-title":"Nat Commun"},{"key":"5032_CR129","doi-asserted-by":"publisher","first-page":"2","DOI":"10.1016\/s0962-8924(97)01187-2","volume":"8","author":"MG Farquhar","year":"1998","unstructured":"Farquhar MG, Palade GE (1998) The Golgi apparatus: 100 years of progress and controversy. Trends Cell Biol 8:2\u201310. https:\/\/doi.org\/10.1016\/s0962-8924(97)01187-2","journal-title":"Trends Cell Biol"},{"key":"5032_CR130","doi-asserted-by":"publisher","first-page":"4949","DOI":"10.1093\/emboj\/18.18.4949","volume":"18","author":"J Shorter","year":"1999","unstructured":"Shorter J, Watson R, Giannakou ME et al (1999) GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system. EMBO J 18:4949\u20134960. https:\/\/doi.org\/10.1093\/emboj\/18.18.4949","journal-title":"EMBO J"},{"key":"5032_CR131","doi-asserted-by":"publisher","first-page":"3279","DOI":"10.1093\/emboj\/cdg317","volume":"22","author":"Y Wang","year":"2003","unstructured":"Wang Y, Seemann J, Pypaert M et al (2003) A direct role for GRASP65 as a mitotically regulated Golgi stacking factor. EMBO J 22:3279\u20133290. https:\/\/doi.org\/10.1093\/emboj\/cdg317","journal-title":"EMBO J"},{"key":"5032_CR132","doi-asserted-by":"publisher","first-page":"296","DOI":"10.1016\/j.tcb.2013.01.008","volume":"23","author":"D Tang","year":"2013","unstructured":"Tang D, Wang Y (2013) Cell cycle regulation of Golgi membrane dynamics. Trends Cell Biol 23:296\u2013304. https:\/\/doi.org\/10.1016\/j.tcb.2013.01.008","journal-title":"Trends Cell Biol"},{"key":"5032_CR133","doi-asserted-by":"publisher","first-page":"237","DOI":"10.1083\/jcb.200907132","volume":"188","author":"Y Xiang","year":"2010","unstructured":"Xiang Y, Wang Y (2010) GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking. J Cell Biol 188:237\u2013251. https:\/\/doi.org\/10.1083\/jcb.200907132","journal-title":"J Cell Biol"},{"key":"5032_CR134","doi-asserted-by":"publisher","first-page":"877","DOI":"10.1083\/jcb.200108079","volume":"155","author":"B Short","year":"2001","unstructured":"Short B, Preisinger C, K\u00f6rner R et al (2001) A GRASP55-rab2 effector complex linking Golgi structure to membrane traffic. J Cell Biol 155:877\u2013883. https:\/\/doi.org\/10.1083\/jcb.200108079","journal-title":"J Cell Biol"},{"key":"5032_CR135","doi-asserted-by":"publisher","first-page":"3567","DOI":"10.1002\/j.1460-2075.1991.tb04923.x","volume":"10","author":"T Nilsson","year":"1991","unstructured":"Nilsson T, Lucocq JM, Mackay D et al (1991) The membrane spanning domain of beta-1,4-galactosyltransferase specifies trans Golgi localization. EMBO J 10:3567\u20133575. https:\/\/doi.org\/10.1002\/j.1460-2075.1991.tb04923.x","journal-title":"EMBO J"},{"key":"5032_CR136","doi-asserted-by":"publisher","first-page":"562","DOI":"10.1002\/j.1460-2075.1994.tb06294.x","volume":"13","author":"T Nilsson","year":"1994","unstructured":"Nilsson T, Hoe MH, Slusarewicz P et al (1994) Kin recognition between medial Golgi enzymes in HeLa cells. EMBO J 13:562\u2013574. https:\/\/doi.org\/10.1002\/j.1460-2075.1994.tb06294.x","journal-title":"EMBO J"},{"key":"5032_CR137","doi-asserted-by":"publisher","first-page":"1617","DOI":"10.1242\/jcs.108.4.1617","volume":"108","author":"C Rabouille","year":"1995","unstructured":"Rabouille C, Hui N, Hunte F et al (1995) Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides. J Cell Sci 108:1617\u20131627","journal-title":"J Cell Sci"},{"key":"5032_CR138","doi-asserted-by":"publisher","first-page":"542","DOI":"10.1016\/S0959-440X(00)00128-7","volume":"10","author":"PM Berninsone","year":"2000","unstructured":"Berninsone PM, Hirschberg CB (2000) Nucleotide sugar transporters of the Golgi apparatus. Curr Opin Struct Biol 10:542\u2013547","journal-title":"Curr Opin Struct Biol"},{"key":"5032_CR139","doi-asserted-by":"publisher","first-page":"631","DOI":"10.1111\/j.1432-1033.1992.tb17090.x","volume":"207","author":"H Shoji","year":"1992","unstructured":"Shoji H, Takahashi N, Nomoto H et al (1992) Detailed structural analysis of asparagine-linked oligosaccharides of the nicotinic acetylcholine receptor from Torpedo californica. Eur J Biochem 207:631\u2013641. https:\/\/doi.org\/10.1111\/j.1432-1033.1992.tb17090.x","journal-title":"Eur J Biochem"},{"key":"5032_CR140","first-page":"661","volume-title":"Methods in enzymology","author":"L Poulter","year":"1990","unstructured":"Poulter L, Burlingame AL (1990) Desorption mass spectrometry of oligosaccharides coupled with hydrophobic chromophores. Methods in enzymology, vol 193. Academic Press, pp 661\u2013689"},{"key":"5032_CR141","doi-asserted-by":"publisher","first-page":"48","DOI":"10.3389\/fnmol.2020.00048","volume":"13","author":"JC Rudell","year":"2020","unstructured":"Rudell JC, Borges LS, Yarov-Yarovoy V et al (2020) The MX-Helix of muscle nAChR subunits regulates receptor assembly and surface trafficking. Front Mol Neurosci 13:48. https:\/\/doi.org\/10.3389\/fnmol.2020.00048","journal-title":"Front Mol Neurosci"},{"key":"5032_CR142","doi-asserted-by":"publisher","first-page":"1800","DOI":"10.1093\/oxfordjournals.molbev.a003967","volume":"18","author":"Z Takacs","year":"2001","unstructured":"Takacs Z, Wilhelmsen KC, Sorota S (2001) Snake \u03b1-neurotoxin binding site on the Egyptian cobra (Naja haje) nicotinic acetylcholine receptor is conserved. Mol Biol Evol 18:1800\u20131809","journal-title":"Mol Biol Evol"},{"key":"5032_CR143","doi-asserted-by":"publisher","first-page":"10691","DOI":"10.1073\/pnas.0703394104","volume":"104","author":"MF Tansky","year":"2007","unstructured":"Tansky MF, Pothoulakis C, Leeman SE (2007) Functional consequences of alteration of N-linked glycosylation sites on the neurokinin 1 receptor. Proc Natl Acad Sci 104:10691\u201310696","journal-title":"Proc Natl Acad Sci"},{"key":"5032_CR144","doi-asserted-by":"publisher","first-page":"1636","DOI":"10.1016\/j.bbamcr.2015.03.017","volume":"1853","author":"L Console","year":"2015","unstructured":"Console L, Scalise M, Tarmakova Z et al (2015) N-linked glycosylation of human SLC1A5 (ASCT2) transporter is critical for trafficking to membrane. Biochim Biophys Acta 1853:1636\u20131645. https:\/\/doi.org\/10.1016\/j.bbamcr.2015.03.017","journal-title":"Biochim Biophys Acta"},{"key":"5032_CR145","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.68910","volume":"10","author":"AP Govind","year":"2021","unstructured":"Govind AP, Jeyifous O, Russell TA et al (2021) Activity-dependent Golgi satellite formation in dendrites reshapes the neuronal surface glycoproteome. Elife 10:e68910","journal-title":"Elife"},{"key":"5032_CR146","doi-asserted-by":"publisher","first-page":"2","DOI":"10.1523\/JNEUROSCI.2484-21.2022","volume":"43","author":"HJ Zhang","year":"2023","unstructured":"Zhang HJ, Zammit M, Kao C-M et al (2023) Trapping of nicotinic acetylcholine receptor ligands assayed by in vitro cellular studies and in vivo PET imaging. J Neurosci 43:2\u201313. https:\/\/doi.org\/10.1523\/JNEUROSCI.2484-21.2022","journal-title":"J Neurosci"},{"key":"5032_CR147","doi-asserted-by":"publisher","first-page":"792","DOI":"10.1016\/j.tcb.2020.07.004","volume":"30","author":"A Valenzuela","year":"2020","unstructured":"Valenzuela A, Meservey L, Nguyen H et al (2020) Golgi outposts nucleate microtubules in cells with specialized shapes. Trends Cell Biol 30:792\u2013804. https:\/\/doi.org\/10.1016\/j.tcb.2020.07.004","journal-title":"Trends Cell Biol"},{"key":"5032_CR148","doi-asserted-by":"publisher","first-page":"3764","DOI":"10.1016\/j.febslet.2009.10.064","volume":"583","author":"T Nilsson","year":"2009","unstructured":"Nilsson T, Au CE, Bergeron JJM (2009) Sorting out glycosylation enzymes in the Golgi apparatus. FEBS Lett 583:3764\u20133769. https:\/\/doi.org\/10.1016\/j.febslet.2009.10.064","journal-title":"FEBS Lett"},{"key":"5032_CR149","doi-asserted-by":"publisher","first-page":"762","DOI":"10.1016\/j.semcdb.2009.03.004","volume":"20","author":"D Ungar","year":"2009","unstructured":"Ungar D (2009) Golgi linked protein glycosylation and associated diseases. Semin Cell Dev Biol 20:762\u2013769. https:\/\/doi.org\/10.1016\/j.semcdb.2009.03.004","journal-title":"Semin Cell Dev Biol"},{"key":"5032_CR150","doi-asserted-by":"publisher","first-page":"2024","DOI":"10.1016\/j.carres.2008.01.034","volume":"343","author":"RD Smith","year":"2008","unstructured":"Smith RD, Lupashin VV (2008) Role of the conserved oligomeric Golgi (COG) complex in protein glycosylation. Carbohydr Res 343:2024\u20132031. https:\/\/doi.org\/10.1016\/j.carres.2008.01.034","journal-title":"Carbohydr Res"},{"key":"5032_CR151","doi-asserted-by":"publisher","first-page":"405","DOI":"10.1083\/jcb.200202016","volume":"157","author":"D Ungar","year":"2002","unstructured":"Ungar D, Oka T, Brittle EE et al (2002) Characterization of a mammalian Golgi-localized protein complex, COG, that is required for normal Golgi morphology and function. J Cell Biol 157:405\u2013415. https:\/\/doi.org\/10.1083\/jcb.200202016","journal-title":"J Cell Biol"},{"key":"5032_CR152","doi-asserted-by":"publisher","first-page":"32729","DOI":"10.1074\/jbc.M504590200","volume":"280","author":"D Ungar","year":"2005","unstructured":"Ungar D, Oka T, Vasile E et al (2005) Subunit architecture of the conserved oligomeric Golgi complex. J Biol Chem 280:32729\u201332735. https:\/\/doi.org\/10.1074\/jbc.M504590200","journal-title":"J Biol Chem"},{"key":"5032_CR153","doi-asserted-by":"publisher","first-page":"270","DOI":"10.1111\/j.1600-0854.2006.00530.x","volume":"8","author":"M Sohda","year":"2007","unstructured":"Sohda M, Misumi Y, Yoshimura SI et al (2007) The interaction of two tethering factors, p115 and COG complex, is required for Golgi integrity. Traffic 8:270\u2013284. https:\/\/doi.org\/10.1111\/j.1600-0854.2006.00530.x","journal-title":"Traffic"},{"key":"5032_CR154","doi-asserted-by":"publisher","first-page":"21025","DOI":"10.1074\/jbc.M002386200","volume":"275","author":"FB Schapiro","year":"2000","unstructured":"Schapiro FB, Grinstein S (2000) Determinants of the pH of the Golgi complex. J Biol Chem 275:21025\u201321032. https:\/\/doi.org\/10.1074\/jbc.M002386200","journal-title":"J Biol Chem"},{"key":"5032_CR155","doi-asserted-by":"publisher","first-page":"521","DOI":"10.1523\/JNEUROSCI.20-02-00521.2000","volume":"20","author":"S Marchand","year":"2000","unstructured":"Marchand S, Bignami F, Stetzkowski-Marden F et al (2000) The myristoylated protein rapsyn is cotargeted with the nicotinic acetylcholine receptor to the postsynaptic membrane via the exocytic pathway. J Neurosci 20:521\u2013528","journal-title":"J Neurosci"},{"key":"5032_CR156","doi-asserted-by":"publisher","first-page":"8891","DOI":"10.1523\/JNEUROSCI.22-20-08891.2002","volume":"22","author":"S Marchand","year":"2002","unstructured":"Marchand S, Devillers-Thi\u00e9ry A, Pons S et al (2002) Rapsyn escorts the nicotinic acetylcholine receptor along the exocytic pathway via association with lipid rafts. J Neurosci 22:8891\u20138901","journal-title":"J Neurosci"},{"key":"5032_CR157","doi-asserted-by":"publisher","first-page":"389","DOI":"10.1146\/annurev.neuro.22.1.389","volume":"22","author":"JR Sanes","year":"1999","unstructured":"Sanes JR, Lichtman JW (1999) Development of the vertebrate neuromuscular junction. Annu Rev Neurosci 22:389\u2013442","journal-title":"Annu Rev Neurosci"},{"key":"5032_CR158","doi-asserted-by":"publisher","first-page":"791","DOI":"10.1038\/35097557","volume":"2","author":"JR Sanes","year":"2001","unstructured":"Sanes JR, Lichtman JW (2001) Induction, assembly, maturation and maintenance of a postsynaptic apparatus. Nat Rev Neurosci 2:791\u2013805","journal-title":"Nat Rev Neurosci"},{"key":"5032_CR159","doi-asserted-by":"publisher","DOI":"10.3389\/fnmol.2021.744597","volume":"14","author":"AS Vall\u00e9s","year":"2021","unstructured":"Vall\u00e9s AS, Barrantes FJ (2021) Dysregulation of neuronal nicotinic acetylcholine receptor-cholesterol crosstalk in autism spectrum disorder. Front Mol Neurosci 14:744597. https:\/\/doi.org\/10.3389\/fnmol.2021.744597","journal-title":"Front Mol Neurosci"},{"key":"5032_CR160","doi-asserted-by":"publisher","DOI":"10.1016\/j.phrs.2023.106729","volume":"190","author":"FJ Barrantes","year":"2023","unstructured":"Barrantes FJ (2023) Structure and function meet at the nicotinic acetylcholine receptor-lipid interface. Pharmacol Res 190:106729. https:\/\/doi.org\/10.1016\/j.phrs.2023.106729","journal-title":"Pharmacol Res"},{"key":"5032_CR161","doi-asserted-by":"publisher","first-page":"1328875","DOI":"10.3389\/fcell.2023.1328875","volume":"11","author":"FJ Barrantes","year":"2023","unstructured":"Barrantes FJ (2023) Modulation of a rapid neurotransmitter receptor-ion channel by membrane lipids. Front Cell Dev Biol 11:1328875. https:\/\/doi.org\/10.3389\/fcell.2023.1328875","journal-title":"Front Cell Dev Biol"},{"key":"5032_CR162","doi-asserted-by":"publisher","first-page":"715","DOI":"10.1083\/jcb.141.3.715","volume":"141","author":"T Meier","year":"1998","unstructured":"Meier T, Masciulli F, Moore C et al (1998) Agrin can mediate acetylcholine receptor gene expression in muscle by aggregation of muscle-derived neuregulins. J Cell Biol 141:715\u2013726","journal-title":"J Cell Biol"},{"key":"5032_CR163","doi-asserted-by":"publisher","first-page":"599","DOI":"10.1126\/science.276.5312.599","volume":"276","author":"AW Sandrock Jr","year":"1997","unstructured":"Sandrock AW Jr, Dryer SE, Rosen KM et al (1997) Maintenance of acetylcholine receptor number by neuregulins at the neuromuscular junction in vivo. Science 276:599\u2013603","journal-title":"Science"},{"key":"5032_CR164","doi-asserted-by":"publisher","first-page":"335","DOI":"10.1093\/emboj\/17.2.335","volume":"17","author":"AJ Denzer","year":"1998","unstructured":"Denzer AJ, Schulthess T, Fauser C et al (1998) Electron microscopic structure of agrin and mapping of its binding site in laminin-1. EMBO J 17:335\u2013343. https:\/\/doi.org\/10.1093\/emboj\/17.2.335","journal-title":"EMBO J"},{"key":"5032_CR165","doi-asserted-by":"publisher","first-page":"673","DOI":"10.1242\/dev.115.3.673","volume":"115","author":"SA Jo","year":"1992","unstructured":"Jo SA, Burden SJ (1992) Synaptic basal lamina contains a signal for synapse-specific transcription. Development 115:673\u2013680","journal-title":"Development"},{"key":"5032_CR166","doi-asserted-by":"publisher","first-page":"158","DOI":"10.1038\/373158a0","volume":"373","author":"SA Jo","year":"1995","unstructured":"Jo SA, Zhu X, Marchionni MA et al (1995) Neuregulins are concentrated at nerve-muscle synapses and activate ACh\u2013receptor gene expression. Nature 373:158\u2013161","journal-title":"Nature"},{"key":"5032_CR167","doi-asserted-by":"publisher","first-page":"79","DOI":"10.1385\/MN:25:1:079","volume":"25","author":"KH Huh","year":"2002","unstructured":"Huh KH, Fuhrer C (2002) Clustering of nicotinic acetylcholine receptors: from the neuromuscular junction to interneuronal synapses. Mol Neurobiol 25:79\u2013112","journal-title":"Mol Neurobiol"},{"key":"5032_CR168","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.49180.001","volume":"8","author":"G Xing","year":"2019","unstructured":"Xing G, Jing H, Zhang L et al (2019) A mechanism in agrin signaling revealed by a prevalent Rapsyn mutation in congenital myasthenic syndrome. Elife 8:e49180. https:\/\/doi.org\/10.7554\/eLife.49180.001","journal-title":"Elife"},{"key":"5032_CR169","doi-asserted-by":"publisher","first-page":"717","DOI":"10.1038\/nn1071","volume":"6","author":"AJ Finn","year":"2003","unstructured":"Finn AJ, Feng G, Pendergast AM (2003) Postsynaptic requirement for Abl kinases in assembly of the neuromuscular junction. Nat Neurosci 6:717\u2013723","journal-title":"Nat Neurosci"},{"key":"5032_CR170","doi-asserted-by":"publisher","first-page":"14505","DOI":"10.1074\/jbc.M007024200","volume":"276","author":"P Mittaud","year":"2001","unstructured":"Mittaud P, Marangi PA, Erb-V\u00f6gtli S et al (2001) Agrin-induced activation of acetylcholine receptor-bound Src family kinases requires Rapsyn and correlates with acetylcholine receptor clustering. J Biol Chem 276:14505\u201314513. https:\/\/doi.org\/10.1074\/jbc.M007024200","journal-title":"J Biol Chem"},{"key":"5032_CR171","doi-asserted-by":"publisher","first-page":"4951","DOI":"10.1093\/emboj\/16.16.4951","volume":"16","author":"C Fuhrer","year":"1997","unstructured":"Fuhrer C, Sugiyama JE, Taylor RG et al (1997) Association of muscle-specific kinase MuSK with the acetylcholine receptor in mammalian muscle. EMBO J 16:4951\u20134960","journal-title":"EMBO J"},{"key":"5032_CR172","doi-asserted-by":"publisher","first-page":"380","DOI":"10.1006\/mcne.2000.0835","volume":"15","author":"N Parkhomovskiy","year":"2000","unstructured":"Parkhomovskiy N, Kammesheidt A, Martin PT (2000) N-acetyllactosamine and the CT carbohydrate antigen mediate agrin-dependent activation of MuSK and acetylcholine receptor clustering in skeletal muscle. Mol Cell Neurosci 15:380\u2013397. https:\/\/doi.org\/10.1006\/mcne.2000.0835","journal-title":"Mol Cell Neurosci"},{"key":"5032_CR173","doi-asserted-by":"publisher","first-page":"20529","DOI":"10.1074\/jbc.274.29.20529","volume":"274","author":"AS Mohamed","year":"1999","unstructured":"Mohamed AS, Swope SL (1999) Phosphorylation and cytoskeletal anchoring of the acetylcholine receptor by Src class protein-tyrosine kinases Activation by rapsyn. J Biol Chem 274:20529\u201320539. https:\/\/doi.org\/10.1074\/jbc.274.29.20529","journal-title":"J Biol Chem"},{"key":"5032_CR174","doi-asserted-by":"publisher","first-page":"5419","DOI":"10.1074\/jbc.273.10.5419","volume":"273","author":"T Okamoto","year":"1998","unstructured":"Okamoto T, Schlegel A, Scherer PE et al (1998) Caveolins, a family of scaffolding proteins for organizing \u2018\u201cpreassembled signaling complexes\u201d\u2019 at the plasma membrane. J Biol Chem 273:5419\u20135422. https:\/\/doi.org\/10.1074\/jbc.273.10.5419","journal-title":"J Biol Chem"},{"key":"5032_CR175","doi-asserted-by":"publisher","first-page":"108","DOI":"10.1016\/0014-5793(95)01256-7","volume":"376","author":"M Way","year":"1995","unstructured":"Way M, Parton RG (1995) M-caveolin, a muscle-specific caveolin-related protein. FEBS Lett 376:108\u2013112. https:\/\/doi.org\/10.1016\/0014-5793(95)01256-7","journal-title":"FEBS Lett"},{"key":"5032_CR176","doi-asserted-by":"publisher","first-page":"2255","DOI":"10.1074\/jbc.271.4.2255","volume":"271","author":"Z Tang","year":"1996","unstructured":"Tang Z, Scherer PE, Okamoto T et al (1996) Molecular cloning of caveolin-3, a novel member of the caveolin gene family expressed predominantly in muscle. J Biol Chem 271:2255\u20132261. https:\/\/doi.org\/10.1074\/jbc.271.4.2255","journal-title":"J Biol Chem"},{"key":"5032_CR177","doi-asserted-by":"publisher","first-page":"205","DOI":"10.1083\/jcb.150.1.205","volume":"150","author":"C Weston","year":"2000","unstructured":"Weston C, Yee B, Hod E et al (2000) Agrin-induced acetylcholine receptor clustering is mediated by the small guanosine triphosphatases Rac and Cdc42. J Cell Biol 150:205\u2013212","journal-title":"J Cell Biol"},{"key":"5032_CR178","doi-asserted-by":"publisher","DOI":"10.3390\/ijms21228736","author":"BS Pradhan","year":"2020","unstructured":"Pradhan BS, Pr\u00f3szy\u0144ski TJ (2020) A role for caveolin-3 in the pathogenesis of muscular dystrophies. Int J Mol Sci. https:\/\/doi.org\/10.3390\/ijms21228736","journal-title":"Int J Mol Sci"},{"key":"5032_CR179","doi-asserted-by":"publisher","first-page":"302","DOI":"10.1091\/mbc.e09-05-0381","volume":"21","author":"M Hezel","year":"2010","unstructured":"Hezel M, de Groat WC, Galbiati F (2010) Caveolin-3 promotes nicotinic acetylcholine receptor clustering and regulates neuromuscular junction activity. Mol Biol Cell 21:302\u2013310","journal-title":"Mol Biol Cell"},{"key":"5032_CR180","doi-asserted-by":"publisher","first-page":"1133","DOI":"10.1083\/jcb.146.5.1133","volume":"146","author":"H Zhou","year":"1999","unstructured":"Zhou H, Glass DJ, Yancopoulos GD et al (1999) Distinct domains of MuSK mediate its abilities to induce and to associate with postsynaptic specializations. J Cell Biol 146:1133\u20131146","journal-title":"J Cell Biol"},{"key":"5032_CR181","doi-asserted-by":"publisher","first-page":"623","DOI":"10.1016\/S0896-6273(00)80303-7","volume":"18","author":"ED Apel","year":"1997","unstructured":"Apel ED, Glass DJ, Moscoso LM et al (1997) Rapsyn is required for MuSK signaling and recruits synaptic components to a MuSK-containing scaffold. Neuron 18:623\u2013635","journal-title":"Neuron"},{"key":"5032_CR182","doi-asserted-by":"publisher","first-page":"3151","DOI":"10.1523\/JNEUROSCI.21-09-03151.2001","volume":"21","author":"CL Smith","year":"2001","unstructured":"Smith CL, Mittaud P, Prescott ED et al (2001) Src, Fyn, and Yes are not required for neuromuscular synapse formation but are necessary for stabilization of agrin-induced clusters of acetylcholine receptors. J Neurosci 21:3151\u20133160","journal-title":"J Neurosci"},{"key":"5032_CR183","doi-asserted-by":"publisher","first-page":"2246","DOI":"10.1242\/jcs.032003","volume":"121","author":"OL Gerv\u00e1sio","year":"2008","unstructured":"Gerv\u00e1sio OL, Whitehead NP, Yeung EW et al (2008) TRPC1 binds to caveolin-3 and is regulated by Src kinase\u2014role in Duchenne muscular dystrophy. J Cell Sci 121:2246\u20132255. https:\/\/doi.org\/10.1242\/jcs.032003","journal-title":"J Cell Sci"},{"key":"5032_CR184","doi-asserted-by":"publisher","first-page":"10479","DOI":"10.1523\/JNEUROSCI.2103-05.2005","volume":"25","author":"G Sadasivam","year":"2005","unstructured":"Sadasivam G, Willmann R, Lin S et al (2005) Src-family kinases stabilize the neuromuscular synapse in vivo via protein interactions, phosphorylation, and cytoskeletal linkage of acetylcholine receptors. J Neurosci 25:10479\u201310493. https:\/\/doi.org\/10.1523\/JNEUROSCI.2103-05.2005","journal-title":"J Neurosci"},{"key":"5032_CR185","doi-asserted-by":"publisher","first-page":"232","DOI":"10.1038\/377232a0","volume":"377","author":"M Gautam","year":"1995","unstructured":"Gautam M, Noakes PG, Mudd J et al (1995) Failure of postsynaptic specialization to develop at neuromuscular junctions of rapsyn-deficient mice. Nature 377:232\u2013236","journal-title":"Nature"},{"key":"5032_CR186","doi-asserted-by":"publisher","first-page":"340","DOI":"10.1006\/mcne.1999.0779","volume":"14","author":"MM Maimone","year":"1999","unstructured":"Maimone MM, Enigk RE (1999) The intracellular domain of the nicotinic acetylcholine receptor \u03b1 subunit mediates its coclustering with rapsyn. Mol Cell Neurosci 14:340\u2013354","journal-title":"Mol Cell Neurosci"},{"key":"5032_CR187","doi-asserted-by":"publisher","first-page":"10622","DOI":"10.1073\/pnas.1301277110","volume":"110","author":"B Zuber","year":"2013","unstructured":"Zuber B, Unwin N (2013) Structure and superorganization of acetylcholine receptor-rapsyn complexes. Proc Natl Acad Sci U S A 110:10622\u201310627. https:\/\/doi.org\/10.1073\/pnas.1301277110","journal-title":"Proc Natl Acad Sci U S A"},{"key":"5032_CR188","doi-asserted-by":"publisher","first-page":"222","DOI":"10.1016\/j.neuroscience.2009.05.057","volume":"163","author":"Y Lee","year":"2009","unstructured":"Lee Y, Rudell J, Ferns M (2009) Rapsyn interacts with the muscle acetylcholine receptor via alpha-helical domains in the alpha, beta, and epsilon subunit intracellular loops. Neuroscience 163:222\u2013232. https:\/\/doi.org\/10.1016\/j.neuroscience.2009.05.057","journal-title":"Neuroscience"},{"key":"5032_CR189","doi-asserted-by":"publisher","first-page":"8190","DOI":"10.1016\/S0021-9258(18)47547-3","volume":"262","author":"WJ LaRochelle","year":"1987","unstructured":"LaRochelle WJ, Froehner SC (1987) Comparison of the postsynaptic 43-kDa protein from muscle cells that differ in acetylcholine receptor clustering activity. J Biol Chem 262:8190\u20138195. https:\/\/doi.org\/10.1016\/S0021-9258(18)47547-3","journal-title":"J Biol Chem"},{"key":"5032_CR190","doi-asserted-by":"publisher","first-page":"4007","DOI":"10.1073\/pnas.95.7.4007","volume":"95","author":"MK Ramarao","year":"1998","unstructured":"Ramarao MK, Cohen JB (1998) Mechanism of nicotinic acetylcholine receptor cluster formation by rapsyn. Proc Natl Acad Sci 95:4007\u20134012","journal-title":"Proc Natl Acad Sci"},{"key":"5032_CR191","doi-asserted-by":"publisher","first-page":"15602","DOI":"10.1016\/S0021-9258(19)37631-8","volume":"263","author":"DE Frail","year":"1988","unstructured":"Frail DE, McLaughlin LL, Mudd J et al (1988) Identification of the mouse muscle 43,000-dalton acetylcholine receptor-associated protein (RAPsyn) by cDNA cloning. J Biol Chem 263:15602\u201315607. https:\/\/doi.org\/10.1016\/S0021-9258(19)37631-8","journal-title":"J Biol Chem"},{"key":"5032_CR192","doi-asserted-by":"publisher","first-page":"7475","DOI":"10.1074\/jbc.M009888200","volume":"276","author":"MK Ramarao","year":"2001","unstructured":"Ramarao MK, Bianchetta MJ, Lanken J et al (2001) Role of rapsyn tetratricopeptide repeat and coiled-coil domains in self-association and nicotinic acetylcholine receptor clustering. J Biol Chem 276:7475\u20137483. https:\/\/doi.org\/10.1074\/jbc.M009888200","journal-title":"J Biol Chem"},{"key":"5032_CR193","doi-asserted-by":"publisher","first-page":"719","DOI":"10.1083\/jcb.123.3.719","volume":"123","author":"PB Scotland","year":"1993","unstructured":"Scotland PB, Colledge M, Melnikova I et al (1993) Clustering of the acetylcholine receptor by the 43-kD protein: involvement of the zinc finger domain. J Cell Biol 123:719\u2013728","journal-title":"J Cell Biol"},{"key":"5032_CR194","doi-asserted-by":"publisher","first-page":"1129","DOI":"10.1002\/bies.20305","volume":"27","author":"L Strochlic","year":"2005","unstructured":"Strochlic L, Cartaud A, Cartaud J (2005) The synaptic muscle-specific kinase (MuSK) complex: new partners, new functions. BioEssays 27:1129\u20131135. https:\/\/doi.org\/10.1002\/bies.20305","journal-title":"BioEssays"},{"key":"5032_CR195","first-page":"51","volume-title":"The Abl family kinases: mechanisms of regulation and signalling. Advances in cancer research","author":"AM Pendergast","year":"2002","unstructured":"Pendergast AM (2002) The Abl family kinases: mechanisms of regulation and signalling. Advances in cancer research, vol 85. Academic Press, pp 51\u2013100"},{"key":"5032_CR196","doi-asserted-by":"publisher","first-page":"489","DOI":"10.1016\/S0896-6273(02)00783-3","volume":"35","author":"ZG Luo","year":"2002","unstructured":"Luo ZG, Wang Q, Zhou JZ et al (2002) Regulation of AChR clustering by dishevelled interacting with MuSK and PAK1. Neuron 35:489\u2013505","journal-title":"Neuron"},{"key":"5032_CR197","doi-asserted-by":"publisher","first-page":"1321","DOI":"10.1083\/jcb.150.6.1321","volume":"150","author":"Z Dai","year":"2000","unstructured":"Dai Z, Luo X, Xie H et al (2000) The actin-driven movement and formation of acetylcholine receptor clusters. J Cell Biol 150:1321\u20131334","journal-title":"J Cell Biol"},{"key":"5032_CR198","doi-asserted-by":"publisher","first-page":"1017","DOI":"10.1038\/nn1128","volume":"6","author":"J Wang","year":"2003","unstructured":"Wang J, Jing Z, Zhang L et al (2003) Regulation of acetylcholine receptor clustering by the tumor suppressor APC. Nat Neurosci 6:1017\u20131018. https:\/\/doi.org\/10.1038\/nn1128","journal-title":"Nat Neurosci"},{"key":"5032_CR199","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/s12035-009-8089-5","volume":"41","author":"GSK Pilgram","year":"2010","unstructured":"Pilgram GSK, Potikanond S, Baines RA et al (2010) The roles of the dystrophin-associated glycoprotein complex at the synapse. Mol Neurobiol 41:1\u201321. https:\/\/doi.org\/10.1007\/s12035-009-8089-5","journal-title":"Mol Neurobiol"},{"key":"5032_CR200","doi-asserted-by":"publisher","first-page":"809","DOI":"10.1083\/jcb.122.4.809","volume":"122","author":"JM Ervasti","year":"1993","unstructured":"Ervasti JM, Campbell KP (1993) A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J Cell Biol 122:809\u2013823","journal-title":"J Cell Biol"},{"key":"5032_CR201","doi-asserted-by":"publisher","first-page":"1575","DOI":"10.1002\/mus.1192","volume":"24","author":"TA Rando","year":"2001","unstructured":"Rando TA (2001) The dystrophin-glycoprotein complex, cellular signaling, and the regulation of cell survival in the muscular dystrophies. Muscle Nerve 24:1575\u20131594. https:\/\/doi.org\/10.1002\/mus.1192","journal-title":"Muscle Nerve"},{"key":"5032_CR202","doi-asserted-by":"publisher","first-page":"663","DOI":"10.1016\/0092-8674(94)90051-5","volume":"77","author":"JT Campanelll","year":"1994","unstructured":"Campanelll JT, Roberds SL, Campbell KP et al (1994) A role for dystrophin-associated glycoproteins and utrophin in agrin-induced AChR clustering. Cell 77:663\u2013674","journal-title":"Cell"},{"key":"5032_CR203","doi-asserted-by":"publisher","first-page":"1614","DOI":"10.1007\/s00018-005-5461-0","volume":"63","author":"T Haenggi","year":"2006","unstructured":"Haenggi T, Fritschy J-M (2006) Role of dystrophin and utrophin for assembly and function of the dystrophin glycoprotein complex in non-muscle tissue. Cell Mol Life Sci 63:1614\u20131631. https:\/\/doi.org\/10.1007\/s00018-005-5461-0","journal-title":"Cell Mol Life Sci"},{"key":"5032_CR204","doi-asserted-by":"publisher","first-page":"1269","DOI":"10.1083\/jcb.142.5.1269","volume":"142","author":"MF Peters","year":"1998","unstructured":"Peters MF, Sadoulet-Puccio HM, Mark Grady R et al (1998) Differential membrane localization and intermolecular associations of \u03b1-dystrobrevin isoforms in skeletal muscle. J Cell Biol 142:1269\u20131278","journal-title":"J Cell Biol"},{"key":"5032_CR205","doi-asserted-by":"publisher","first-page":"499","DOI":"10.1016\/0896-6273(91)90301-F","volume":"7","author":"K Ohlendieck","year":"1991","unstructured":"Ohlendieck K, Ervasti JM, Matsumura K et al (1991) Dystrophin-related protein is localized to neuromuscular junctions of adult skeletal muscle. Neuron 7:499\u2013508","journal-title":"Neuron"},{"key":"5032_CR206","doi-asserted-by":"publisher","first-page":"24911","DOI":"10.1074\/jbc.M103258200","volume":"276","author":"M Bartoli","year":"2001","unstructured":"Bartoli M, Ramarao MK, Cohen JB (2001) Interactions of the rapsyn RING-H2 domain with dystroglycan. J Biol Chem 276:24911\u201324917. https:\/\/doi.org\/10.1074\/jbc.M103258200","journal-title":"J Biol Chem"},{"key":"5032_CR207","doi-asserted-by":"publisher","first-page":"1749","DOI":"10.1016\/S0002-9440(10)65046-8","volume":"156","author":"CI Raats","year":"2000","unstructured":"Raats CI, van den Born J, Bakker MA et al (2000) Expression of agrin, dystroglycan, and utrophin in normal renal tissue and in experimental glomerulopathies. Am J Pathol 156:1749\u20131765","journal-title":"Am J Pathol"},{"key":"5032_CR208","doi-asserted-by":"publisher","first-page":"15425","DOI":"10.1074\/jbc.270.25.15425","volume":"270","author":"NR Smalheiser","year":"1995","unstructured":"Smalheiser NR, Kim E (1995) Purification of cranin, a laminin binding membrane protein. Identity with dystroglycan and reassessment of its carbohydrate moieties. J Biol Chem 270:15425\u201315433. https:\/\/doi.org\/10.1074\/jbc.270.25.15425","journal-title":"J Biol Chem"},{"key":"5032_CR209","doi-asserted-by":"publisher","first-page":"743","DOI":"10.1016\/0896-6273(95)90218-X","volume":"14","author":"PT Martin","year":"1995","unstructured":"Martin PT, Sanes JR (1995) Role for a synapse-specific carbohydrate in agrin-induced clustering of acetylcholine receptors. Neuron 14:743\u2013754","journal-title":"Neuron"},{"key":"5032_CR210","doi-asserted-by":"publisher","first-page":"646","DOI":"10.1038\/300646a0","volume":"300","author":"JR Sanes","year":"1982","unstructured":"Sanes JR, Cheney JM (1982) Lectin binding reveals a synapse-specific carbohydrate in skeletal muscle. Nature 300:646\u2013647","journal-title":"Nature"},{"key":"5032_CR211","doi-asserted-by":"publisher","first-page":"932","DOI":"10.1523\/JNEUROSCI.08-03-00932.1988","volume":"8","author":"LJ Scott","year":"1988","unstructured":"Scott LJ, Bacou F, Sanes JR (1988) A synapse-specific carbohydrate at the neuromuscular junction: association with both acetylcholinesterase and a glycolipid. J Neurosci 8:932\u2013944","journal-title":"J Neurosci"},{"key":"5032_CR212","doi-asserted-by":"publisher","first-page":"22315","DOI":"10.1074\/jbc.272.35.22315","volume":"272","author":"JM Ervasti","year":"1997","unstructured":"Ervasti JM, Burwell AL, Geissler AL (1997) Tissue-specific heterogeneity in alpha-dystroglycan sialoglycosylation. Skeletal muscle alpha-dystroglycan is a latent receptor for Vicia villosa agglutinin b4 masked by sialic acid modification. J Biol Chem 272:22315\u201322321. https:\/\/doi.org\/10.1074\/jbc.272.35.22315","journal-title":"J Biol Chem"},{"key":"5032_CR213","doi-asserted-by":"publisher","first-page":"1757","DOI":"10.1016\/j.cell.2019.04.017","volume":"177","author":"CR Shurer","year":"2019","unstructured":"Shurer CR, Kuo JCH, Roberts LM et al (2019) Physical principles of membrane shape regulation by the glycocalyx. Cell 177:1757-1770.e21. https:\/\/doi.org\/10.1016\/j.cell.2019.04.017","journal-title":"Cell"},{"key":"5032_CR214","doi-asserted-by":"publisher","first-page":"38048","DOI":"10.1074\/jbc.M005321200","volume":"275","author":"F Sotgia","year":"2000","unstructured":"Sotgia F, Lee JK, Das K et al (2000) Caveolin-3 directly interacts with the C-terminal tail of beta-dystroglycan. Identification of a central WW-like domain within caveolin family members. J Biol Chem 275:38048\u201338058. https:\/\/doi.org\/10.1074\/jbc.M005321200","journal-title":"J Biol Chem"},{"key":"5032_CR215","doi-asserted-by":"publisher","first-page":"165","DOI":"10.1152\/physrev.1979.59.1.165","volume":"59","author":"DM Fambrough","year":"1979","unstructured":"Fambrough DM (1979) Control of acetylcholine receptors in skeletal muscle. Physiol Rev 59:165\u2013227","journal-title":"Physiol Rev"},{"key":"5032_CR216","doi-asserted-by":"publisher","first-page":"511","DOI":"10.1146\/annurev.biochem.66.1.511","volume":"66","author":"SL Schmid","year":"1997","unstructured":"Schmid SL (1997) Clathrin-coated vesicle formation and protein sorting: an integrated process. Annu Rev Biochem 66:511\u2013548","journal-title":"Annu Rev Biochem"},{"key":"5032_CR217","doi-asserted-by":"publisher","first-page":"395","DOI":"10.1146\/annurev.biochem.72.121801.161800","volume":"72","author":"JS Bonifacino","year":"2003","unstructured":"Bonifacino JS, Traub LM (2003) Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu Rev Biochem 72:395\u2013447. https:\/\/doi.org\/10.1146\/annurev.biochem.72.121801.161800","journal-title":"Annu Rev Biochem"},{"key":"5032_CR218","doi-asserted-by":"publisher","first-page":"141","DOI":"10.1146\/annurev.cellbio.19.110701.154617","volume":"19","author":"L Hicke","year":"2003","unstructured":"Hicke L, Dunn R (2003) Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu Rev Cell Dev Biol 19:141\u2013172. https:\/\/doi.org\/10.1146\/annurev.cellbio.19.110701.154617","journal-title":"Annu Rev Cell Dev Biol"},{"key":"5032_CR219","doi-asserted-by":"publisher","first-page":"1307","DOI":"10.1126\/science.1063866","volume":"294","author":"SK Shenoy","year":"2001","unstructured":"Shenoy SK, McDonald PH, Kohout TA et al (2001) Regulation of receptor fate by ubiquitination of activated \u03b22-adrenergic receptor and \u03b2-arrestin. Science 294:1307\u20131313","journal-title":"Science"},{"key":"5032_CR220","first-page":"7876","volume":"14","author":"T Arnason","year":"1994","unstructured":"Arnason T, Ellison MJ (1994) Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain. Mol Cell Biol 14:7876\u20137883","journal-title":"Mol Cell Biol"},{"key":"5032_CR221","doi-asserted-by":"publisher","first-page":"94","DOI":"10.1093\/emboj\/19.1.94","volume":"19","author":"JS Thrower","year":"2000","unstructured":"Thrower JS, Hoffman L, Rechsteiner M et al (2000) Recognition of the polyubiquitin proteolytic signal. EMBO J 19:94\u2013102. https:\/\/doi.org\/10.1093\/emboj\/19.1.94","journal-title":"EMBO J"},{"key":"5032_CR222","doi-asserted-by":"publisher","first-page":"28497","DOI":"10.1074\/jbc.M805092200","volume":"283","author":"N Lineberry","year":"2008","unstructured":"Lineberry N, Su L, Soares L et al (2008) The single subunit transmembrane E3 ligase gene related to anergy in lymphocytes (GRAIL) captures and then ubiquitinates transmembrane proteins across the cell membrane. J Biol Chem 283:28497\u201328505. https:\/\/doi.org\/10.1074\/jbc.M805092200","journal-title":"J Biol Chem"},{"key":"5032_CR223","doi-asserted-by":"publisher","first-page":"527","DOI":"10.1016\/S0955-0674(97)80029-4","volume":"9","author":"LM Traub","year":"1997","unstructured":"Traub LM, Kornfeld S (1997) The trans-Golgi network: a late secretory sorting station. Curr Opin Cell Biol 9:527\u2013533","journal-title":"Curr Opin Cell Biol"},{"key":"5032_CR224","doi-asserted-by":"publisher","first-page":"839","DOI":"10.1046\/j.1460-9568.1998.00091.x","volume":"10","author":"G Camus","year":"1998","unstructured":"Camus G, Jasmin BJ, Cartaud J (1998) Polarized sorting of nicotinic acetylcholine receptors to the postsynaptic membrane in torpedo electrocyte. Eur J Neurosci 10:839\u2013852","journal-title":"Eur J Neurosci"},{"key":"5032_CR225","doi-asserted-by":"publisher","first-page":"231","DOI":"10.1146\/annurev-biochem-060210-093619","volume":"81","author":"JA MacGurn","year":"2012","unstructured":"MacGurn JA, Hsu PC, Emr SD (2012) Ubiquitin and membrane protein turnover: from cradle to grave. Annu Rev Biochem 81:231\u2013259. https:\/\/doi.org\/10.1146\/annurev-biochem-060210-093619","journal-title":"Annu Rev Biochem"},{"key":"5032_CR226","doi-asserted-by":"publisher","first-page":"18","DOI":"10.1186\/s40035-015-0041-1","volume":"4","author":"YB Hu","year":"2015","unstructured":"Hu YB, Dammer EB, Ren RJ et al (2015) The endosomal-lysosomal system: from acidification and cargo sorting to neurodegeneration. Transl Neurodegener 4:18. https:\/\/doi.org\/10.1186\/s40035-015-0041-1","journal-title":"Transl Neurodegener"},{"key":"5032_CR227","doi-asserted-by":"publisher","DOI":"10.1101\/cshperspect.a016774","volume":"6","author":"C Burd","year":"2014","unstructured":"Burd C, Cullen PJ (2014) Retromer: a master conductor of endosome sorting. Cold Spring Harb Perspect Biol 6:a016774. https:\/\/doi.org\/10.1101\/cshperspect.a016774","journal-title":"Cold Spring Harb Perspect Biol"},{"key":"5032_CR228","doi-asserted-by":"publisher","first-page":"427","DOI":"10.1016\/j.ceb.2008.03.009","volume":"20","author":"JS Bonifacino","year":"2008","unstructured":"Bonifacino JS, Hurley JH (2008) Retromer. Curr Opin Cell Biol 20:427\u2013436. https:\/\/doi.org\/10.1016\/j.ceb.2008.03.009","journal-title":"Curr Opin Cell Biol"},{"key":"5032_CR229","doi-asserted-by":"publisher","first-page":"127","DOI":"10.1016\/j.pneurobio.2011.10.002","volume":"97","author":"X Li","year":"2012","unstructured":"Li X, DiFiglia M (2012) The recycling endosome and its role in neurological disorders. Prog Neurobiol 97:127\u2013141. https:\/\/doi.org\/10.1016\/j.pneurobio.2011.10.002","journal-title":"Prog Neurobiol"},{"key":"5032_CR230","doi-asserted-by":"publisher","first-page":"497","DOI":"10.1016\/j.cell.2010.03.011","volume":"141","author":"D Poteryaev","year":"2010","unstructured":"Poteryaev D, Datta S, Ackema K et al (2010) Identification of the switch in early-to-late endosome transition. Cell 141:497\u2013508. https:\/\/doi.org\/10.1016\/j.cell.2010.03.011","journal-title":"Cell"},{"key":"5032_CR231","doi-asserted-by":"publisher","first-page":"240","DOI":"10.1111\/jnc.12676","volume":"129","author":"D Villarroel-Campos","year":"2014","unstructured":"Villarroel-Campos D, Gastaldi L, Conde C et al (2014) Rab-mediated trafficking role in neurite formation. J Neurochem 129:240\u2013248. https:\/\/doi.org\/10.1111\/jnc.12676","journal-title":"J Neurochem"},{"issue":"12","key":"5032_CR232","doi-asserted-by":"publisher","first-page":"2905","DOI":"10.1242\/jcs.109.12.2905","volume":"109","author":"TE Tjelle","year":"1996","unstructured":"Tjelle TE, Brech A, Juvet LK et al (1996) Isolation and characterization of early endosomes, late endosomes and terminal lysosomes: their role in protein degradation. J Cell Sci 109(12):2905\u20132914","journal-title":"J Cell Sci"},{"key":"5032_CR233","doi-asserted-by":"publisher","first-page":"417","DOI":"10.1042\/bj3630417","volume":"363","author":"CS Pillay","year":"2002","unstructured":"Pillay CS, Elliott E, Dennison C (2002) Endolysosomal proteolysis and its regulation. Biochem J 363:417\u2013429","journal-title":"Biochem J"},{"key":"5032_CR234","doi-asserted-by":"publisher","first-page":"297","DOI":"10.1016\/j.molonc.2009.06.004","volume":"3","author":"N Fehrenbacher","year":"2009","unstructured":"Fehrenbacher N, Bar-Sagi D, Philips M (2009) Ras\/MAPK signaling from endomembranes. Mol Oncol 3:297\u2013307. https:\/\/doi.org\/10.1016\/j.molonc.2009.06.004","journal-title":"Mol Oncol"},{"key":"5032_CR235","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/S0092-8674(01)00428-7","volume":"106","author":"PP Di Fiore","year":"2001","unstructured":"Di Fiore PP, de Camilli P (2001) Endocytosis and signaling: an inseparable partnership. Cell 106:1\u20134","journal-title":"Cell"},{"key":"5032_CR236","doi-asserted-by":"publisher","first-page":"285","DOI":"10.1078\/0171-9335-00160","volume":"80","author":"MP Oksvold","year":"2001","unstructured":"Oksvold MP, Skarpen E, Wier\u00f8d L et al (2001) Re-localization of activated EGF receptor and its signal transducers to multivesicular compartments downstream of early endosomes in response to EGF. Eur J Cell Biol 80:285\u2013294. https:\/\/doi.org\/10.1078\/0171-9335-00160","journal-title":"Eur J Cell Biol"},{"key":"5032_CR237","doi-asserted-by":"publisher","first-page":"679","DOI":"10.1016\/j.molcel.2006.02.011","volume":"21","author":"N Jura","year":"2006","unstructured":"Jura N, Scotto-Lavino E, Sobczyk A et al (2006) Differential modification of Ras proteins by ubiquitination. Mol Cell 21:679\u2013687. https:\/\/doi.org\/10.1016\/j.molcel.2006.02.011","journal-title":"Mol Cell"},{"key":"5032_CR238","doi-asserted-by":"publisher","first-page":"1461","DOI":"10.1242\/jcs.042267","volume":"122","author":"H Yan","year":"2009","unstructured":"Yan H, Chin ML, Horvath EA et al (2009) Impairment of ubiquitylation by mutation in Drosophila E1 promotes both cell-autonomous and non-cell-autonomous Ras-ERK activation in vivo. J Cell Sci 122:1461\u20131470. https:\/\/doi.org\/10.1242\/jcs.042267","journal-title":"J Cell Sci"}],"container-title":["Molecular and Cellular Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11010-024-05032-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s11010-024-05032-x\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11010-024-05032-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,7,17]],"date-time":"2024-07-17T08:07:14Z","timestamp":1721203634000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s11010-024-05032-x"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,5,21]]},"references-count":238,"journal-issue":{"issue":"7","published-print":{"date-parts":[[2024,7]]}},"alternative-id":["5032"],"URL":"https:\/\/doi.org\/10.1007\/s11010-024-05032-x","relation":{},"ISSN":["0300-8177","1573-4919"],"issn-type":[{"value":"0300-8177","type":"print"},{"value":"1573-4919","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,5,21]]},"assertion":[{"value":"22 January 2024","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"4 May 2024","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"21 May 2024","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"The authors declare that they have no competing interests.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}},{"value":"Not applicable.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics approval"}},{"value":"Not applicable.","order":4,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent to participate"}},{"value":"Not applicable.","order":5,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent for publication"}}]}}