{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,8]],"date-time":"2026-11-08T02:49:00Z","timestamp":1794106140580,"version":"4.8.0"},"reference-count":98,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2023,11,22]],"date-time":"2023-11-22T00:00:00Z","timestamp":1700611200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2023,11,22]],"date-time":"2023-11-22T00:00:00Z","timestamp":1700611200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"name":"National Health and Medical Research Council of Australia","award":["10305133"],"award-info":[{"award-number":["10305133"]}]},{"name":"National Health and Medical Research Council of Australia","award":["1086887"],"award-info":[{"award-number":["1086887"]}]},{"name":"National Health and Medical Research Council of Australia","award":["1095215"],"award-info":[{"award-number":["1095215"]}]},{"name":"National Health and Medical Research Council of Australia","award":["10305133"],"award-info":[{"award-number":["10305133"]}]},{"name":"National Health and Medical Research Council of Australia","award":["1086887"],"award-info":[{"award-number":["1086887"]}]},{"name":"National Health and Medical Research Council of Australia","award":["1095215"],"award-info":[{"award-number":["1095215"]}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Sci Rep"],"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Amyotrophic lateral sclerosis (ALS) is a severely debilitating neurodegenerative condition that is part of the same disease spectrum as frontotemporal dementia (FTD). Mutations in the <jats:italic>CCNF<\/jats:italic> gene, encoding cyclin F, are present in both sporadic and familial ALS and FTD. However, the pathophysiological mechanisms underlying neurodegeneration remain unclear. Proper functioning of the endoplasmic reticulum (ER) and Golgi apparatus compartments is essential for normal physiological activities and to maintain cellular viability. Here, we demonstrate that ALS\/FTD-associated variant cyclin F<jats:sup>S621G<\/jats:sup> inhibits secretory protein transport from the ER to Golgi apparatus, by a mechanism involving dysregulation of COPII vesicles at ER exit sites. Consistent with this finding, cyclin F<jats:sup>S621G<\/jats:sup> also induces fragmentation of the Golgi apparatus and activates ER stress, ER-associated degradation, and apoptosis. Induction of Golgi fragmentation and ER stress were confirmed with a second ALS\/FTD variant cyclin F<jats:sup>S195R<\/jats:sup>, and in cortical primary neurons. Hence, this study provides novel insights into pathogenic mechanisms associated with ALS\/FTD-variant cyclin F, involving perturbations to both secretory protein trafficking and ER-Golgi homeostasis.<\/jats:p>","DOI":"10.1038\/s41598-023-46802-9","type":"journal-article","created":{"date-parts":[[2023,11,22]],"date-time":"2023-11-22T12:03:04Z","timestamp":1700654584000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["ALS\/FTD-associated mutation in cyclin F inhibits ER-Golgi trafficking, inducing ER stress, ERAD and Golgi fragmentation"],"prefix":"10.1038","volume":"13","author":[{"given":"Audrey M. G.","family":"Ragagnin","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vinod","family":"Sundaramoorthy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fabiha","family":"Farzana","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shashi","family":"Gautam","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sayanthooran","family":"Saravanabavan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zeinab","family":"Takalloo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Prachi","family":"Mehta","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dzung","family":"Do-Ha","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sonam","family":"Parakh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sina","family":"Shadfar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Julie","family":"Hunter","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marta","family":"Vidal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cyril J.","family":"Jagaraj","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mariana","family":"Brocardo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anna","family":"Konopka","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shu","family":"Yang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stephanie L.","family":"Rayner","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kelly L.","family":"Williams","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ian P.","family":"Blair","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roger S.","family":"Chung","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Albert","family":"Lee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lezanne","family":"Ooi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2427-499X","authenticated-orcid":false,"given":"Julie D.","family":"Atkin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2023,11,22]]},"reference":[{"key":"46802_CR1","doi-asserted-by":"publisher","first-page":"245","DOI":"10.1016\/j.neuron.2011.09.011","volume":"72","author":"M DeJesus-Hernandez","year":"2011","unstructured":"DeJesus-Hernandez, M. et al. Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS. Neuron 72, 245\u2013256. https:\/\/doi.org\/10.1016\/j.neuron.2011.09.011 (2011).","journal-title":"Neuron"},{"key":"46802_CR2","doi-asserted-by":"publisher","first-page":"257","DOI":"10.1016\/j.neuron.2011.09.010","volume":"72","author":"AE Renton","year":"2011","unstructured":"Renton, A. E. et al. A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD. Neuron 72, 257\u2013268. https:\/\/doi.org\/10.1016\/j.neuron.2011.09.010 (2011).","journal-title":"Neuron"},{"key":"46802_CR3","doi-asserted-by":"publisher","first-page":"11253","DOI":"10.1038\/ncomms11253","volume":"7","author":"KL Williams","year":"2016","unstructured":"Williams, K. L. et al. CCNF mutations in amyotrophic lateral sclerosis and frontotemporal dementia. Nat. Commun. 7, 11253. https:\/\/doi.org\/10.1038\/ncomms11253 (2016).","journal-title":"Nat. Commun."},{"key":"46802_CR4","doi-asserted-by":"publisher","first-page":"135","DOI":"10.1016\/j.tcb.2012.10.011","volume":"23","author":"V D\u2019Angiolella","year":"2013","unstructured":"D\u2019Angiolella, V., Esencay, M. & Pagano, M. A cyclin without cyclin-dependent kinases: Cyclin F controls genome stability through ubiquitin-mediated proteolysis. Trends Cell Biol. 23, 135\u2013140. https:\/\/doi.org\/10.1016\/j.tcb.2012.10.011 (2013).","journal-title":"Trends Cell Biol."},{"key":"46802_CR5","doi-asserted-by":"publisher","first-page":"6087","DOI":"10.1002\/j.1460-2075.1994.tb06955.x","volume":"13","author":"C Bai","year":"1994","unstructured":"Bai, C., Richman, R. & Elledge, S. J. Human cyclin F. EMBO J. 13, 6087\u20136098 (1994).","journal-title":"EMBO J."},{"key":"46802_CR6","doi-asserted-by":"publisher","first-page":"138","DOI":"10.1038\/nature09140","volume":"466","author":"V D\u2019Angiolella","year":"2010","unstructured":"D\u2019Angiolella, V. et al. SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity through CP110 degradation. Nature 466, 138\u2013142. https:\/\/doi.org\/10.1038\/nature09140 (2010).","journal-title":"Nature"},{"key":"46802_CR7","doi-asserted-by":"publisher","first-page":"369","DOI":"10.1038\/nrm3582","volume":"14","author":"JR Skaar","year":"2013","unstructured":"Skaar, J. R., Pagan, J. K. & Pagano, M. Mechanisms and function of substrate recruitment by F-box proteins. Nat. Rev. Mol. Cell Biol. 14, 369\u2013381. https:\/\/doi.org\/10.1038\/nrm3582 (2013).","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"46802_CR8","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1152\/physrev.00012.2016","volume":"97","author":"N Foot","year":"2017","unstructured":"Foot, N., Henshall, T. & Kumar, S. Ubiquitination and the regulation of membrane proteins. Physiol. Rev. 97, 253\u2013281. https:\/\/doi.org\/10.1152\/physrev.00012.2016 (2017).","journal-title":"Physiol. Rev."},{"key":"46802_CR9","doi-asserted-by":"publisher","first-page":"170058","DOI":"10.1098\/rsob.170058","volume":"7","author":"A Lee","year":"2017","unstructured":"Lee, A. et al. Casein kinase II phosphorylation of cyclin F at serine 621 regulates the Lys48-ubiquitylation E3 ligase activity of the SCF(cyclin F) complex. Open Biol. 7, 170058. https:\/\/doi.org\/10.1098\/rsob.170058 (2017).","journal-title":"Open Biol."},{"key":"46802_CR10","doi-asserted-by":"publisher","first-page":"335","DOI":"10.1007\/s00018-017-2632-8","volume":"75","author":"A Lee","year":"2018","unstructured":"Lee, A. et al. Pathogenic mutation in the ALS\/FTD gene, CCNF, causes elevated Lys48-linked ubiquitylation and defective autophagy. Cell Mol. Life Sci. CMLS 75, 335\u2013354. https:\/\/doi.org\/10.1007\/s00018-017-2632-8 (2018).","journal-title":"Cell Mol. Life Sci. CMLS"},{"key":"46802_CR11","doi-asserted-by":"publisher","first-page":"2616","DOI":"10.1093\/hmg\/ddx136","volume":"26","author":"AL Hogan","year":"2017","unstructured":"Hogan, A. L. et al. Expression of ALS\/FTD-linked mutant CCNF in zebrafish leads to increased cell death in the spinal cord and an aberrant motor phenotype. Hum. Mol. Genet. 26, 2616\u20132626. https:\/\/doi.org\/10.1093\/hmg\/ddx136 (2017).","journal-title":"Hum. Mol. Genet."},{"key":"46802_CR12","doi-asserted-by":"publisher","first-page":"123","DOI":"10.3389\/fnmol.2017.00123","volume":"10","author":"CP Webster","year":"2017","unstructured":"Webster, C. P., Smith, E. F., Shaw, P. J. & De Vos, K. J. Protein homeostasis in amyotrophic lateral sclerosis: Therapeutic opportunities?. Front Mol. Neurosci. 10, 123. https:\/\/doi.org\/10.3389\/fnmol.2017.00123 (2017).","journal-title":"Front Mol. Neurosci."},{"key":"46802_CR13","doi-asserted-by":"publisher","first-page":"119","DOI":"10.3389\/fnmol.2017.00119","volume":"10","author":"H Shahheydari","year":"2017","unstructured":"Shahheydari, H. et al. Protein quality control and the amyotrophic lateral sclerosis\/frontotemporal dementia continuum. Front Mol. Neurosci. 10, 119. https:\/\/doi.org\/10.3389\/fnmol.2017.00119 (2017).","journal-title":"Front Mol. Neurosci."},{"key":"46802_CR14","doi-asserted-by":"publisher","first-page":"679","DOI":"10.1007\/s00401-015-1468-2","volume":"130","author":"KY Soo","year":"2015","unstructured":"Soo, K. Y. et al. Rab1-dependent ER-Golgi transport dysfunction is a common pathogenic mechanism in SOD1, TDP-43 and FUS-associated ALS. Acta Neuropathol. (Berl.) 130, 679\u2013697. https:\/\/doi.org\/10.1007\/s00401-015-1468-2 (2015).","journal-title":"Acta Neuropathol. (Berl.)"},{"key":"46802_CR15","doi-asserted-by":"publisher","first-page":"3859","DOI":"10.1007\/s00018-019-03394-w","volume":"77","author":"M Halloran","year":"2020","unstructured":"Halloran, M. et al. Amyotrophic lateral sclerosis-linked UBQLN2 mutants inhibit endoplasmic reticulum to Golgi transport, leading to Golgi fragmentation and ER stress. Cell Mol. Life Sci. CMLS 77, 3859\u20133873. https:\/\/doi.org\/10.1007\/s00018-019-03394-w (2020).","journal-title":"Cell Mol. Life Sci. CMLS"},{"key":"46802_CR16","doi-asserted-by":"publisher","first-page":"377","DOI":"10.1038\/ncb1371","volume":"8","author":"D Zeuschner","year":"2006","unstructured":"Zeuschner, D. et al. Immuno-electron tomography of ER exit sites reveals the existence of free COPII-coated transport carriers. Nat. Cell Biol. 8, 377\u2013383 (2006).","journal-title":"Nat. Cell Biol."},{"key":"46802_CR17","doi-asserted-by":"publisher","first-page":"875","DOI":"10.1083\/jcb.131.4.875","volume":"131","author":"M Aridor","year":"1995","unstructured":"Aridor, M., Bannykh, S. I., Rowe, T. & Balch, W. E. Sequential coupling between COPII and COPI vesicle coats in endoplasmic reticulum to Golgi transport. J. Cell Biol. 131, 875\u2013893 (1995).","journal-title":"J. Cell Biol."},{"key":"46802_CR18","doi-asserted-by":"publisher","first-page":"940","DOI":"10.1016\/j.tcb.2019.08.007","volume":"29","author":"J McCaughey","year":"2019","unstructured":"McCaughey, J. & Stephens, D. J. ER-to-Golgi transport: A sizeable problem. Trends Cell Biol. 29, 940\u2013953. https:\/\/doi.org\/10.1016\/j.tcb.2019.08.007 (2019).","journal-title":"Trends Cell Biol."},{"key":"46802_CR19","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. Protein sorting at the ER\u2013Golgi interface protein sorting in the ER and Golgi. J. Cell Biol. 215, 769\u2013778. https:\/\/doi.org\/10.1083\/jcb.201610031 (2016).","journal-title":"J. Cell Biol."},{"key":"46802_CR20","doi-asserted-by":"publisher","first-page":"495","DOI":"10.1038\/nature10822","volume":"482","author":"L Jin","year":"2012","unstructured":"Jin, L. et al. Ubiquitin-dependent regulation of COPII coat size and function. Nature 482, 495\u2013500. https:\/\/doi.org\/10.1038\/nature10822 (2012).","journal-title":"Nature"},{"key":"46802_CR21","doi-asserted-by":"publisher","first-page":"861","DOI":"10.1111\/j.1600-0854.2008.00729.x","volume":"9","author":"K Nakatsukasa","year":"2008","unstructured":"Nakatsukasa, K. & Brodsky, J. L. The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum. Traffic Cph Den. 9, 861\u2013870. https:\/\/doi.org\/10.1111\/j.1600-0854.2008.00729.x (2008).","journal-title":"Traffic Cph Den."},{"key":"46802_CR22","doi-asserted-by":"publisher","first-page":"369","DOI":"10.1111\/j.1600-0854.2007.00542.x","volume":"8","author":"S Mukherjee","year":"2007","unstructured":"Mukherjee, S., Chiu, R., Leung, S.-M. & Shields, D. Fragmentation of the Golgi apparatus: An early apoptotic event independent of the cytoskeleton. Traffic Cph Den. 8, 369\u2013378. https:\/\/doi.org\/10.1111\/j.1600-0854.2007.00542.x (2007).","journal-title":"Traffic Cph Den."},{"key":"46802_CR23","doi-asserted-by":"publisher","first-page":"748","DOI":"10.3390\/cells8070748","volume":"8","author":"J\u00c1 Mart\u00ednez-Men\u00e1rguez","year":"2019","unstructured":"Mart\u00ednez-Men\u00e1rguez, J. \u00c1., Tom\u00e1s, M., Mart\u00ednez-Mart\u00ednez, N. & Mart\u00ednez-Alonso, E. Golgi fragmentation in neurodegenerative diseases: Is there a common cause?. Cells 8, 748 (2019).","journal-title":"Cells"},{"key":"46802_CR24","doi-asserted-by":"publisher","first-page":"7330","DOI":"10.1016\/S0021-9258(18)68646-6","volume":"263","author":"RN Sifers","year":"1988","unstructured":"Sifers, R. N. et al. A frameshift mutation results in a truncated alpha 1-antitrypsin that is retained within the rough endoplasmic reticulum. J. Biol. Chem. 263, 7330\u20137335 (1988).","journal-title":"J. Biol. Chem."},{"key":"46802_CR25","doi-asserted-by":"publisher","first-page":"3393","DOI":"10.1073\/pnas.1300328110","volume":"110","author":"JE Grotzke","year":"2013","unstructured":"Grotzke, J. E., Lu, Q. & Cresswell, P. Deglycosylation-dependent fluorescent proteins provide unique tools for the study of ER-associated degradation. Proc. Natl. Acad. Sci. U. S. A. 110, 3393\u20133398. https:\/\/doi.org\/10.1073\/pnas.1300328110 (2013).","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"46802_CR26","doi-asserted-by":"publisher","DOI":"10.1042\/AN20110031","author":"KA Hosie","year":"2012","unstructured":"Hosie, K. A. et al. Chronic excitotoxin-induced axon degeneration in a compartmented neuronal culture model. ASN Neuro https:\/\/doi.org\/10.1042\/AN20110031 (2012).","journal-title":"ASN Neuro"},{"key":"46802_CR27","doi-asserted-by":"publisher","first-page":"101530","DOI":"10.1016\/j.scr.2019.101530","volume":"40","author":"M Bax","year":"2019","unstructured":"Bax, M. et al. Generation and characterization of a human induced pluripotent stem cell line UOWi005-A from dermal fibroblasts derived from a CCNFS621G familial amyotrophic lateral sclerosis patient using mRNA reprogramming. Stem. Cell Res. 40, 101530. https:\/\/doi.org\/10.1016\/j.scr.2019.101530 (2019).","journal-title":"Stem. Cell Res."},{"key":"46802_CR28","doi-asserted-by":"publisher","first-page":"6626","DOI":"10.1038\/ncomms7626","volume":"6","author":"Z-W Du","year":"2015","unstructured":"Du, Z.-W. et al. Generation and expansion of highly pure motor neuron progenitors from human pluripotent stem cells. Nat. Commun. 6, 6626. https:\/\/doi.org\/10.1038\/ncomms7626 (2015).","journal-title":"Nat. Commun."},{"key":"46802_CR29","doi-asserted-by":"publisher","first-page":"997","DOI":"10.1083\/jcb.200408135","volume":"167","author":"D Xu","year":"2004","unstructured":"Xu, D. & Hay, J. C. 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 (2004).","journal-title":"J. Cell Biol."},{"key":"46802_CR30","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1111\/j.1365-2818.2006.01706.x","volume":"224","author":"S Bolte","year":"2006","unstructured":"Bolte, S. & Cordeli\u00e8res, F. P. A guided tour into subcellular colocalization analysis in light microscopy. J. Microsc. 224, 213\u2013232. https:\/\/doi.org\/10.1111\/j.1365-2818.2006.01706.x (2006).","journal-title":"J. Microsc."},{"key":"46802_CR31","doi-asserted-by":"publisher","first-page":"778","DOI":"10.1101\/pdb.prot087205","volume":"2016","author":"L Crowley","year":"2016","unstructured":"Crowley, L., Marfell, B. & Waterhouse, N. Analyzing cell death by nuclear staining with Hoechst 33342. Cold Spring Harb. Protoc. 2016, 778\u2013781. https:\/\/doi.org\/10.1101\/pdb.prot087205 (2016).","journal-title":"Cold Spring Harb. Protoc."},{"key":"46802_CR32","doi-asserted-by":"publisher","first-page":"81","DOI":"10.1038\/38001","volume":"389","author":"JF Presley","year":"1997","unstructured":"Presley, J. F. et al. ER-to-Golgi transport visualized in living cells. Nature 389, 81\u201385. https:\/\/doi.org\/10.1038\/38001 (1997).","journal-title":"Nature"},{"key":"46802_CR33","doi-asserted-by":"publisher","first-page":"288","DOI":"10.1038\/35010558","volume":"2","author":"S Nehls","year":"2000","unstructured":"Nehls, S. et al. Dynamics and retention of misfolded proteins in native ER membranes. Nat. Cell Biol. 2, 288\u2013295. https:\/\/doi.org\/10.1038\/35010558 (2000).","journal-title":"Nat. Cell Biol."},{"key":"46802_CR34","doi-asserted-by":"publisher","first-page":"3859","DOI":"10.1007\/s00018-019-03394-w","volume":"77","author":"M Halloran","year":"2020","unstructured":"Halloran, M. et al. Amyotrophic lateral sclerosis-linked UBQLN2 mutants inhibit endoplasmic reticulum to Golgi transport, leading to Golgi fragmentation and ER stress. Cell Mol. Life Sci. 77, 3859\u20133873. https:\/\/doi.org\/10.1007\/s00018-019-03394-w (2020).","journal-title":"Cell Mol. Life Sci."},{"key":"46802_CR35","doi-asserted-by":"publisher","first-page":"374","DOI":"10.1128\/JVI.54.2.374-382.1985","volume":"54","author":"CJ Gallione","year":"1985","unstructured":"Gallione, C. J. & Rose, J. K. A single amino acid substitution in a hydrophobic domain causes temperature-sensitive cell-surface transport of a mutant viral glycoprotein. J. Virol. 54, 374\u2013382. https:\/\/doi.org\/10.1128\/JVI.54.2.374-382.1985 (1985).","journal-title":"J. Virol."},{"key":"46802_CR36","doi-asserted-by":"publisher","first-page":"119","DOI":"10.1007\/s00418-018-1689-2","volume":"150","author":"J McCaughey","year":"2018","unstructured":"McCaughey, J. & Stephens, D. J. COPII-dependent ER export in animal cells: Adaptation and control for diverse cargo. Histochem. Cell Biol. 150, 119\u2013131. https:\/\/doi.org\/10.1007\/s00418-018-1689-2 (2018).","journal-title":"Histochem. Cell Biol."},{"key":"46802_CR37","doi-asserted-by":"publisher","first-page":"2727","DOI":"10.1242\/jcs.046680","volume":"122","author":"SS Stylli","year":"2009","unstructured":"Stylli, S. S. et al. Nck adaptor proteins link Tks5 to invadopodia actin regulation and ECM degradation. J. Cell Sci. 122, 2727\u20132740. https:\/\/doi.org\/10.1242\/jcs.046680 (2009).","journal-title":"J. Cell Sci."},{"key":"46802_CR38","doi-asserted-by":"publisher","first-page":"14121","DOI":"10.1074\/jbc.M300659200","volume":"278","author":"AP Joglekar","year":"2003","unstructured":"Joglekar, A. P. et al. The SNARE motif contributes to rbet1 intracellular targeting and dynamics independently of SNARE interactions. J. Biol. Chem. 278, 14121\u201314133. https:\/\/doi.org\/10.1074\/jbc.M300659200 (2003).","journal-title":"J. Biol. Chem."},{"key":"46802_CR39","doi-asserted-by":"publisher","first-page":"3052","DOI":"10.1242\/jcs.028696","volume":"121","author":"DC Prosser","year":"2008","unstructured":"Prosser, D. C. et al. FFAT rescues VAPA-mediated inhibition of ER-to-Golgi transport and VAPB-mediated ER aggregation. J. Cell Sci. 121, 3052\u20133061. https:\/\/doi.org\/10.1242\/jcs.028696 (2008).","journal-title":"J. Cell Sci."},{"key":"46802_CR40","doi-asserted-by":"publisher","first-page":"258","DOI":"10.1016\/s0076-6879(02)51852-8","volume":"351","author":"Y Shimoni","year":"2002","unstructured":"Shimoni, Y. & Schekman, R. Vesicle budding from endoplasmic reticulum. Methods Enzymol. 351, 258\u2013278. https:\/\/doi.org\/10.1016\/s0076-6879(02)51852-8 (2002).","journal-title":"Methods Enzymol."},{"key":"46802_CR41","doi-asserted-by":"publisher","first-page":"3796","DOI":"10.1016\/j.febslet.2009.10.038","volume":"583","author":"A Budnik","year":"2009","unstructured":"Budnik, A. & Stephens, D. J. ER exit sites\u2013localization and control of COPII vesicle formation. FEBS Lett. 583, 3796\u20133803. https:\/\/doi.org\/10.1016\/j.febslet.2009.10.038 (2009).","journal-title":"FEBS Lett."},{"key":"46802_CR42","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1242\/jcs.069773","volume":"124","author":"D Jensen","year":"2011","unstructured":"Jensen, D. & Schekman, R. COPII-mediated vesicle formation at a glance. J. Cell Sci. 124, 1\u20134. https:\/\/doi.org\/10.1242\/jcs.069773 (2011).","journal-title":"J. Cell Sci."},{"key":"46802_CR43","doi-asserted-by":"publisher","first-page":"111","DOI":"10.1016\/j.semcdb.2018.09.013","volume":"93","author":"AB Mehrtash","year":"2019","unstructured":"Mehrtash, A. B. & Hochstrasser, M. Ubiquitin-dependent protein degradation at the endoplasmic reticulum and nuclear envelope. Semin. Cell Dev. Biol. 93, 111\u2013124. https:\/\/doi.org\/10.1016\/j.semcdb.2018.09.013 (2019).","journal-title":"Semin. Cell Dev. Biol."},{"key":"46802_CR44","doi-asserted-by":"publisher","first-page":"22","DOI":"10.1016\/j.ceb.2018.04.004","volume":"53","author":"X Wu","year":"2018","unstructured":"Wu, X. & Rapoport, T. A. Mechanistic insights into ER-associated protein degradation. Curr. Opin. Cell Biol. 53, 22\u201328. https:\/\/doi.org\/10.1016\/j.ceb.2018.04.004 (2018).","journal-title":"Curr. Opin. Cell Biol."},{"key":"46802_CR45","doi-asserted-by":"publisher","first-page":"26287","DOI":"10.1074\/jbc.M303395200","volume":"278","author":"N Hosokawa","year":"2003","unstructured":"Hosokawa, N. et al. Enhancement of endoplasmic reticulum (ER) degradation of misfolded Null Hong Kong alpha1-antitrypsin by human ER mannosidase I. J. Biol. Chem. 278, 26287\u201326294. https:\/\/doi.org\/10.1074\/jbc.M303395200 (2003).","journal-title":"J. Biol. Chem."},{"key":"46802_CR46","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1093\/brain\/awp267","volume":"133","author":"AK Walker","year":"2010","unstructured":"Walker, A. K. et al. Protein disulphide isomerase protects against protein aggregation and is S-nitrosylated in amyotrophic lateral sclerosis. Brain 133, 105\u2013116. https:\/\/doi.org\/10.1093\/brain\/awp267 (2010).","journal-title":"Brain"},{"key":"46802_CR47","doi-asserted-by":"publisher","first-page":"71","DOI":"10.1016\/B978-0-12-385114-7.00004-0","volume":"490","author":"CM Oslowski","year":"2011","unstructured":"Oslowski, C. M. & Urano, F. Measuring ER stress and the unfolded protein response using mammalian tissue culture system. Methods Enzymol. 490, 71\u201392. https:\/\/doi.org\/10.1016\/B978-0-12-385114-7.00004-0 (2011).","journal-title":"Methods Enzymol."},{"key":"46802_CR48","doi-asserted-by":"publisher","DOI":"10.1042\/BSR20170898","author":"S Alam","year":"2017","unstructured":"Alam, S. et al. Sigmar1 regulates endoplasmic reticulum stress-induced C\/EBP-homologous protein expression in cardiomyocytes. Biosci. Rep. https:\/\/doi.org\/10.1042\/BSR20170898 (2017)."},{"key":"46802_CR49","doi-asserted-by":"publisher","first-page":"3083","DOI":"10.3389\/fimmu.2018.03083","volume":"9","author":"H Hu","year":"2018","unstructured":"Hu, H., Tian, M., Ding, C. & Yu, S. The C\/EBP homologous protein (CHOP) transcription factor functions in endoplasmic reticulum stress-induced apoptosis and microbial infection. Front Immunol. 9, 3083. https:\/\/doi.org\/10.3389\/fimmu.2018.03083 (2018).","journal-title":"Front Immunol."},{"key":"46802_CR50","doi-asserted-by":"publisher","first-page":"187","DOI":"10.3389\/fnmol.2017.00187","volume":"10","author":"P Remondelli","year":"2017","unstructured":"Remondelli, P. & Renna, M. The endoplasmic reticulum unfolded protein response in neurodegenerative disorders and its potential therapeutic significance. Front Mol. Neurosci. 10, 187. https:\/\/doi.org\/10.3389\/fnmol.2017.00187 (2017).","journal-title":"Front Mol. Neurosci."},{"key":"46802_CR51","doi-asserted-by":"publisher","first-page":"421","DOI":"10.3389\/fnins.2015.00421","volume":"9","author":"CE Machamer","year":"2015","unstructured":"Machamer, C. E. The Golgi complex in stress and death. Front Neurosci. 9, 421. https:\/\/doi.org\/10.3389\/fnins.2015.00421 (2015).","journal-title":"Front Neurosci."},{"key":"46802_CR52","doi-asserted-by":"publisher","first-page":"406","DOI":"10.1016\/j.bbamcr.2005.03.002","volume":"1744","author":"SW Hicks","year":"2005","unstructured":"Hicks, S. W. & Machamer, C. E. Golgi structure in stress sensing and apoptosis. Biochim. Biophys. Acta 1744, 406\u2013414. https:\/\/doi.org\/10.1016\/j.bbamcr.2005.03.002 (2005).","journal-title":"Biochim. Biophys. Acta"},{"key":"46802_CR53","doi-asserted-by":"publisher","first-page":"2760","DOI":"10.1016\/S0021-9258(18)45944-3","volume":"267","author":"R Persson","year":"1992","unstructured":"Persson, R., Schnell, C. R., Borg, L. A. & Fries, E. Accumulation of Golgi-processed secretory proteins in an organelle of high density upon reduction of ATP concentration in rat hepatocytes. J. Biol. Chem. 267, 2760\u20132766 (1992).","journal-title":"J. Biol. Chem."},{"key":"46802_CR54","doi-asserted-by":"publisher","first-page":"747","DOI":"10.1083\/jcb.200412003","volume":"168","author":"SN Zolov","year":"2005","unstructured":"Zolov, S. N. & Lupashin, V. V. Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells. J. Cell Biol. 168, 747\u2013759 (2005).","journal-title":"J. Cell Biol."},{"key":"46802_CR55","doi-asserted-by":"publisher","first-page":"11721","DOI":"10.1128\/JVI.01355-13","volume":"87","author":"Z Zhou","year":"2013","unstructured":"Zhou, Z. et al. Foot-and-mouth disease virus 3C protease induces fragmentation of the Golgi compartment and blocks intra-Golgi transport. J. Virol. 87, 11721\u201311729 (2013).","journal-title":"J. Virol."},{"key":"46802_CR56","doi-asserted-by":"publisher","first-page":"448","DOI":"10.3389\/fnins.2015.00448","volume":"9","author":"G Haase","year":"2015","unstructured":"Haase, G. & Rabouille, C. Golgi fragmentation in ALS motor neurons. New mechanisms targeting microtubules, tethers, and transport vesicles. Front Neurosci. 9, 448. https:\/\/doi.org\/10.3389\/fnins.2015.00448 (2015).","journal-title":"Front Neurosci."},{"key":"46802_CR57","doi-asserted-by":"publisher","first-page":"346","DOI":"10.1073\/pnas.1608576114","volume":"114","author":"C Liu","year":"2017","unstructured":"Liu, C. et al. Loss of the golgin GM130 causes Golgi disruption, Purkinje neuron loss, and ataxia in mice. Proc. Natl. Acad. Sci. U. S. A. 114, 346\u2013351. https:\/\/doi.org\/10.1073\/pnas.1608576114 (2017).","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"46802_CR58","doi-asserted-by":"publisher","first-page":"409","DOI":"10.1038\/s41467-019-14038-9","volume":"11","author":"A Eisenberg-Lerner","year":"2020","unstructured":"Eisenberg-Lerner, A. et al. Golgi organization is regulated by proteasomal degradation. Nat. Commun. 11, 409. https:\/\/doi.org\/10.1038\/s41467-019-14038-9 (2020).","journal-title":"Nat. Commun."},{"key":"46802_CR59","doi-asserted-by":"publisher","DOI":"10.1101\/pdb.prot087205","author":"LC Crowley","year":"2016","unstructured":"Crowley, L. C., Marfell, B. J. & Waterhouse, N. J. Analyzing cell death by nuclear staining with Hoechst 33342. Cold Spring Harb. Protoc. https:\/\/doi.org\/10.1101\/pdb.prot087205 (2016).","journal-title":"Cold Spring Harb. Protoc."},{"key":"46802_CR60","doi-asserted-by":"publisher","first-page":"94","DOI":"10.1016\/j.semcdb.2017.06.024","volume":"80","author":"F Brandizzi","year":"2018","unstructured":"Brandizzi, F. Transport from the endoplasmic reticulum to the Golgi in plants: Where are we now?. Semin. Cell Dev. Biol. 80, 94\u2013105. https:\/\/doi.org\/10.1016\/j.semcdb.2017.06.024 (2018).","journal-title":"Semin. Cell Dev. Biol."},{"key":"46802_CR61","doi-asserted-by":"publisher","first-page":"2043","DOI":"10.1038\/emboj.2008.136","volume":"27","author":"H Farhan","year":"2008","unstructured":"Farhan, H. et al. Adaptation of endoplasmic reticulum exit sites to acute and chronic increases in cargo load. EMBO J. 27, 2043\u20132054. https:\/\/doi.org\/10.1038\/emboj.2008.136 (2008).","journal-title":"EMBO J."},{"key":"46802_CR62","doi-asserted-by":"publisher","first-page":"525","DOI":"10.1016\/j.cell.2016.09.026","volume":"167","author":"CA McGourty","year":"2016","unstructured":"McGourty, C. A. et al. Regulation of the CUL3 ubiquitin ligase by a calcium-dependent co-adaptor. Cell 167, 525-538.e14. https:\/\/doi.org\/10.1016\/j.cell.2016.09.026 (2016).","journal-title":"Cell"},{"key":"46802_CR63","doi-asserted-by":"publisher","first-page":"635","DOI":"10.1016\/j.bbrc.2018.03.202","volume":"499","author":"K Kawaguchi","year":"2018","unstructured":"Kawaguchi, K. et al. Ubiquitin-specific protease 8 deubiquitinates Sec31A and decreases large COPII carriers and collagen IV secretion. Biochem. Biophys. Res. Commun. 499, 635\u2013641. https:\/\/doi.org\/10.1016\/j.bbrc.2018.03.202 (2018).","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"46802_CR64","doi-asserted-by":"publisher","first-page":"1223","DOI":"10.1007\/s00018-008-8561-9","volume":"66","author":"T Hubert","year":"2009","unstructured":"Hubert, T., Grimal, S., Carroll, P. & Fichard-Carroll, A. Collagens in the developing and diseased nervous system. Cell Mol. Life Sci. CMLS 66, 1223\u20131238. https:\/\/doi.org\/10.1007\/s00018-008-8561-9 (2009).","journal-title":"Cell Mol. Life Sci. CMLS"},{"key":"46802_CR65","doi-asserted-by":"publisher","first-page":"215","DOI":"10.1016\/s0945-053x(01)00134-2","volume":"20","author":"M Sund","year":"2001","unstructured":"Sund, M. et al. Distinct expression of type XIII collagen in neuronal structures and other tissues during mouse development. Matrix Biol. J. Int. Soc. Matrix Biol. 20, 215\u2013231. https:\/\/doi.org\/10.1016\/s0945-053x(01)00134-2 (2001).","journal-title":"Matrix Biol. J. Int. Soc. Matrix Biol."},{"key":"46802_CR66","doi-asserted-by":"publisher","first-page":"229","DOI":"10.1002\/cne.22228","volume":"518","author":"J Su","year":"2010","unstructured":"Su, J., Gorse, K., Ramirez, F. & Fox, M. A. Collagen XIX is expressed by interneurons and contributes to the formation of hippocampal synapses. J. Comp. Neurol. 518, 229\u2013253. https:\/\/doi.org\/10.1002\/cne.22228 (2010).","journal-title":"J. Comp. Neurol."},{"key":"46802_CR67","doi-asserted-by":"publisher","first-page":"dmm032946","DOI":"10.1242\/dmm.032946","volume":"11","author":"I Gregorio","year":"2018","unstructured":"Gregorio, I., Braghetta, P., Bonaldo, P. & Cescon, M. Collagen VI in healthy and diseased nervous system. Dis. Model Mech. 11, dmm032946. https:\/\/doi.org\/10.1242\/dmm.032946 (2018).","journal-title":"Dis. Model Mech."},{"key":"46802_CR68","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1016\/j.cell.2007.02.035","volume":"129","author":"MA Fox","year":"2007","unstructured":"Fox, M. A. et al. Distinct target-derived signals organize formation, maturation, and maintenance of motor nerve terminals. Cell 129, 179\u2013193. https:\/\/doi.org\/10.1016\/j.cell.2007.02.035 (2007).","journal-title":"Cell"},{"key":"46802_CR69","doi-asserted-by":"publisher","first-page":"1192","DOI":"10.1038\/ng1876","volume":"38","author":"SA Boyadjiev","year":"2006","unstructured":"Boyadjiev, S. A. et al. Cranio-lenticulo-sutural dysplasia is caused by a SEC23A mutation leading to abnormal endoplasmic-reticulum-to-Golgi trafficking. Nat. Genet. 38, 1192\u20131197. https:\/\/doi.org\/10.1038\/ng1876 (2006).","journal-title":"Nat. Genet."},{"key":"46802_CR70","doi-asserted-by":"publisher","first-page":"4244","DOI":"10.1074\/jbc.M113.479980","volume":"289","author":"LGD Fryer","year":"2014","unstructured":"Fryer, L. G. D. et al. The endoplasmic reticulum coat protein II transport machinery coordinates cellular lipid secretion and cholesterol biosynthesis. J. Biol. Chem. 289, 4244\u20134261. https:\/\/doi.org\/10.1074\/jbc.M113.479980 (2014).","journal-title":"J. Biol. Chem."},{"key":"46802_CR71","doi-asserted-by":"publisher","first-page":"1451","DOI":"10.1101\/gad.1640108","volume":"22","author":"H Nishitoh","year":"2008","unstructured":"Nishitoh, H. et al. ALS-linked mutant SOD1 induces ER stress- and ASK1-dependent motor neuron death by targeting Derlin-1. Genes Dev. 22, 1451\u20131464. https:\/\/doi.org\/10.1101\/gad.1640108 (2008).","journal-title":"Genes Dev."},{"key":"46802_CR72","doi-asserted-by":"publisher","first-page":"190","DOI":"10.1111\/jnc.12493","volume":"129","author":"JD Atkin","year":"2014","unstructured":"Atkin, J. D. et al. Mutant SOD1 inhibits ER-Golgi transport in amyotrophic lateral sclerosis. J. Neurochem. 129, 190\u2013204. https:\/\/doi.org\/10.1111\/jnc.12493 (2014).","journal-title":"J. Neurochem."},{"key":"46802_CR73","doi-asserted-by":"publisher","first-page":"1437","DOI":"10.1016\/S0021-9258(17)42277-0","volume":"269","author":"C Dascher","year":"1994","unstructured":"Dascher, C. & Balch, W. E. Dominant inhibitory mutants of ARF1 block endoplasmic reticulum to Golgi transport and trigger disassembly of the Golgi apparatus. J. Biol. Chem. 269, 1437\u20131448 (1994).","journal-title":"J. Biol. Chem."},{"key":"46802_CR74","doi-asserted-by":"publisher","first-page":"557","DOI":"10.1083\/jcb.125.3.557","volume":"125","author":"BS Wilson","year":"1994","unstructured":"Wilson, B. S. et al. A Rab1 mutant affecting guanine nucleotide exchange promotes disassembly of the Golgi apparatus. J. Cell Biol. 125, 557\u2013571 (1994).","journal-title":"J. Cell Biol."},{"key":"46802_CR75","doi-asserted-by":"publisher","first-page":"e81170","DOI":"10.1371\/journal.pone.0081170","volume":"8","author":"AK Walker","year":"2013","unstructured":"Walker, A. K. et al. ALS-associated TDP-43 induces endoplasmic reticulum stress, which drives cytoplasmic TDP-43 accumulation and stress granule formation. PLoS ONE 8, e81170. https:\/\/doi.org\/10.1371\/journal.pone.0081170 (2013).","journal-title":"PLoS ONE"},{"key":"46802_CR76","doi-asserted-by":"publisher","first-page":"2855","DOI":"10.1016\/j.neurobiolaging.2012.02.009","volume":"33","author":"MA Farg","year":"2012","unstructured":"Farg, M. A. et al. Mutant FUS induces endoplasmic reticulum stress in amyotrophic lateral sclerosis and interacts with protein disulfide-isomerase. Neurobiol. Aging 33, 2855\u20132868. https:\/\/doi.org\/10.1016\/j.neurobiolaging.2012.02.009 (2012).","journal-title":"Neurobiol. Aging"},{"key":"46802_CR77","doi-asserted-by":"publisher","first-page":"126","DOI":"10.1080\/21678421.2016.1218517","volume":"18","author":"JA Fifita","year":"2017","unstructured":"Fifita, J. A. et al. A novel amyotrophic lateral sclerosis mutation in OPTN induces ER stress and Golgi fragmentation in vitro. Amyotroph. Lateral Scler Front Degener 18, 126\u2013133. https:\/\/doi.org\/10.1080\/21678421.2016.1218517 (2017).","journal-title":"Amyotroph. Lateral Scler Front Degener"},{"key":"46802_CR78","doi-asserted-by":"publisher","first-page":"4181","DOI":"10.1007\/s00018-013-1385-2","volume":"70","author":"V Sundaramoorthy","year":"2013","unstructured":"Sundaramoorthy, V. et al. Extracellular wildtype and mutant SOD1 induces ER-Golgi pathology characteristic of amyotrophic lateral sclerosis in neuronal cells. Cell Mol. Life Sci. CMLS 70, 4181\u20134195. https:\/\/doi.org\/10.1007\/s00018-013-1385-2 (2013).","journal-title":"Cell Mol. Life Sci. CMLS"},{"key":"46802_CR79","doi-asserted-by":"publisher","first-page":"1057","DOI":"10.1001\/archneurol.2011.178","volume":"68","author":"H-X Deng","year":"2011","unstructured":"Deng, H.-X. et al. Differential involvement of optineurin in amyotrophic lateral sclerosis with or without SOD1 mutations. Arch. Neurol. 68, 1057\u20131061. https:\/\/doi.org\/10.1001\/archneurol.2011.178 (2011).","journal-title":"Arch. Neurol."},{"key":"46802_CR80","doi-asserted-by":"publisher","first-page":"12384","DOI":"10.1074\/jbc.M900992200","volume":"284","author":"MA Gitcho","year":"2009","unstructured":"Gitcho, M. A. et al. VCP mutations causing frontotemporal lobar degeneration disrupt localization of TDP-43 and induce cell death. J. Biol. Chem. 284, 12384\u201312398. https:\/\/doi.org\/10.1074\/jbc.M900992200 (2009).","journal-title":"J. Biol. Chem."},{"key":"46802_CR81","doi-asserted-by":"publisher","first-page":"30223","DOI":"10.1074\/jbc.M605049200","volume":"281","author":"K Kanekura","year":"2006","unstructured":"Kanekura, K., Nishimoto, I., Aiso, S. & Matsuoka, M. Characterization of amyotrophic lateral sclerosis-linked P56S mutation of vesicle-associated membrane protein-associated protein B (VAPB\/ALS8). J. Biol. Chem. 281, 30223\u201330233. https:\/\/doi.org\/10.1074\/jbc.M605049200 (2006).","journal-title":"J. Biol. Chem."},{"key":"46802_CR82","doi-asserted-by":"publisher","first-page":"1517","DOI":"10.1093\/hmg\/ddn040","volume":"17","author":"C Gkogkas","year":"2008","unstructured":"Gkogkas, C. et al. VAPB interacts with and modulates the activity of ATF6. Hum. Mol. Genet. 17, 1517\u20131526. https:\/\/doi.org\/10.1093\/hmg\/ddn040 (2008).","journal-title":"Hum. Mol. Genet."},{"key":"46802_CR83","doi-asserted-by":"publisher","first-page":"505","DOI":"10.1007\/s00401-014-1336-5","volume":"128","author":"Y-J Zhang","year":"2014","unstructured":"Zhang, Y.-J. et al. Aggregation-prone c9FTD\/ALS poly(GA) RAN-translated proteins cause neurotoxicity by inducing ER stress. Acta Neuropathol. (Berl.) 128, 505\u2013524. https:\/\/doi.org\/10.1007\/s00401-014-1336-5 (2014).","journal-title":"Acta Neuropathol. (Berl.)"},{"key":"46802_CR84","doi-asserted-by":"publisher","DOI":"10.3390\/ijms21155369","author":"A Lopata","year":"2020","unstructured":"Lopata, A. et al. Ubiquitination in the ERAD Process. Int. J. Mol. Sci. https:\/\/doi.org\/10.3390\/ijms21155369 (2020).","journal-title":"Int. J. Mol. Sci."},{"key":"46802_CR85","doi-asserted-by":"publisher","first-page":"445","DOI":"10.1042\/BCJ20160582","volume":"474","author":"GM Preston","year":"2017","unstructured":"Preston, G. M. & Brodsky, J. L. The evolving role of ubiquitin modification in endoplasmic reticulum-associated degradation. Biochem. J. 474, 445\u2013469. https:\/\/doi.org\/10.1042\/BCJ20160582 (2017).","journal-title":"Biochem. J."},{"key":"46802_CR86","doi-asserted-by":"publisher","first-page":"2169","DOI":"10.1083\/jcb.107.6.2169","volume":"107","author":"LY Chang","year":"1988","unstructured":"Chang, L. Y., Slot, J. W., Geuze, H. J. & Crapo, J. D. Molecular immunocytochemistry of the CuZn superoxide dismutase in rat hepatocytes. J. Cell Biol. 107, 2169\u20132179 (1988).","journal-title":"J. Cell Biol."},{"key":"46802_CR87","doi-asserted-by":"publisher","first-page":"3486","DOI":"10.1093\/hmg\/ddz119","volume":"28","author":"Y Yu","year":"2019","unstructured":"Yu, Y. et al. Pathogenic mutations in the ALS gene CCNF cause cytoplasmic mislocalization of Cyclin F and elevated VCP ATPase activity. Hum. Mol. Genet. 28, 3486\u20133497. https:\/\/doi.org\/10.1093\/hmg\/ddz119 (2019).","journal-title":"Hum. Mol. Genet."},{"key":"46802_CR88","doi-asserted-by":"publisher","first-page":"400","DOI":"10.3389\/fnins.2015.00400","volume":"9","author":"V Sundaramoorthy","year":"2015","unstructured":"Sundaramoorthy, V., Sultana, J. M. & Atkin, J. D. Golgi fragmentation in amyotrophic lateral sclerosis, an overview of possible triggers and consequences. Front Neurosci. 9, 400. https:\/\/doi.org\/10.3389\/fnins.2015.00400 (2015).","journal-title":"Front Neurosci."},{"key":"46802_CR89","doi-asserted-by":"publisher","first-page":"171","DOI":"10.3389\/fcell.2019.00171","volume":"7","author":"J Saraste","year":"2019","unstructured":"Saraste, J. & Prydz, K. A new look at the functional organization of the Golgi ribbon. Front Cell Dev. Biol. 7, 171. https:\/\/doi.org\/10.3389\/fcell.2019.00171 (2019).","journal-title":"Front Cell Dev. Biol."},{"key":"46802_CR90","doi-asserted-by":"publisher","first-page":"137","DOI":"10.1016\/S0022-510X(00)00265-3","volume":"174","author":"Y Fujita","year":"2000","unstructured":"Fujita, Y. et al. Fragmentation of the Golgi apparatus of the anterior horn cells in patients with familial amyotrophic lateral sclerosis with SOD1 mutations and posterior column involvement. J. Neurol. Sci. 174, 137\u2013140 (2000).","journal-title":"J. Neurol. Sci."},{"key":"46802_CR91","doi-asserted-by":"publisher","first-page":"63","DOI":"10.1016\/S0022-510X(99)00301-9","volume":"173","author":"A Stieber","year":"2000","unstructured":"Stieber, A. et al. The neuronal Golgi apparatus is fragmented in transgenic mice expressing a mutant human SOD1, but not in mice expressing the human NF-H gene. J. Neurol. Sci. 173, 63\u201372 (2000).","journal-title":"J. Neurol. Sci."},{"key":"46802_CR92","doi-asserted-by":"publisher","first-page":"38","DOI":"10.1186\/2051-5960-2-38","volume":"2","author":"V van Dis","year":"2014","unstructured":"van Dis, V. et al. Golgi fragmentation precedes neuromuscular denervation and is associated with endosome abnormalities in SOD1-ALS mouse motor neurons. Acta Neuropathol. Commun. 2, 38. https:\/\/doi.org\/10.1186\/2051-5960-2-38 (2014).","journal-title":"Acta Neuropathol. Commun."},{"key":"46802_CR93","doi-asserted-by":"publisher","first-page":"557","DOI":"10.1146\/annurev.cellbio.16.1.557","volume":"16","author":"J Lippincott-Schwartz","year":"2000","unstructured":"Lippincott-Schwartz, J., Roberts, T. H. & Hirschberg, K. Secretory protein trafficking and organelle dynamics in living cells. Annu. Rev. Cell Dev. Biol. 16, 557\u2013589 (2000).","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"46802_CR94","doi-asserted-by":"publisher","first-page":"1505","DOI":"10.1083\/jcb.143.6.1505","volume":"143","author":"B Storrie","year":"1998","unstructured":"Storrie, B. et al. Recycling of Golgi-resident glycosyltransferases through the ER reveals a novel pathway and provides an explanation for nocodazole-induced Golgi scattering. J. Cell Biol. 143, 1505\u20131521 (1998).","journal-title":"J. Cell Biol."},{"key":"46802_CR95","doi-asserted-by":"publisher","first-page":"1595","DOI":"10.1091\/mbc.e06-10-0886","volume":"18","author":"P Marra","year":"2007","unstructured":"Marra, P. et al. The biogenesis of the Golgi ribbon: The roles of membrane input from the ER and of GM130. Mol. Biol. Cell 18, 1595\u20131608 (2007).","journal-title":"Mol. Biol. Cell"},{"key":"46802_CR96","doi-asserted-by":"publisher","first-page":"1976","DOI":"10.1091\/mbc.e07-10-0989","volume":"19","author":"S Mitrovic","year":"2008","unstructured":"Mitrovic, S. et al. The cargo receptors Surf4, endoplasmic reticulum-Golgi intermediate compartment (ERGIC)-53, and p25 are required to maintain the architecture of ERGIC and Golgi. Mol. Biol. Cell 19, 1976\u20131990 (2008).","journal-title":"Mol. Biol. Cell"},{"key":"46802_CR97","doi-asserted-by":"publisher","first-page":"5011","DOI":"10.1091\/mbc.e03-06-0437","volume":"14","author":"S Puri","year":"2003","unstructured":"Puri, S. & Linstedt, A. D. Capacity of the Golgi apparatus for biogenesis from the endoplasmic reticulum. Mol. Biol. Cell 14, 5011\u20135018 (2003).","journal-title":"Mol. Biol. Cell"},{"key":"46802_CR98","doi-asserted-by":"publisher","first-page":"1223","DOI":"10.1038\/nmeth.f.404","volume":"14","author":"J Huff","year":"2017","unstructured":"Huff, J. et al. The new 2D superresolution mode for ZEISS airyscan. Nat. Methods 14, 1223\u20131223. https:\/\/doi.org\/10.1038\/nmeth.f.404 (2017).","journal-title":"Nat. Methods"}],"container-title":["Scientific Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41598-023-46802-9.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-023-46802-9","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-023-46802-9.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,11,22]],"date-time":"2023-11-22T12:08:46Z","timestamp":1700654926000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41598-023-46802-9"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,11,22]]},"references-count":98,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2023,12]]}},"alternative-id":["46802"],"URL":"https:\/\/doi.org\/10.1038\/s41598-023-46802-9","relation":{"references":[{"id-type":"uri","id":"","asserted-by":"subject"}]},"ISSN":["2045-2322"],"issn-type":[{"value":"2045-2322","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,11,22]]},"assertion":[{"value":"3 April 2023","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"5 November 2023","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"22 November 2023","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"20467"}}