{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T14:23:29Z","timestamp":1790519009990,"version":"4.1.0"},"reference-count":38,"publisher":"National Academy of Sciences","issue":"45","license":[{"start":{"date-parts":[[2017,10,23]],"date-time":"2017-10-23T00:00:00Z","timestamp":1508716800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/www.pnas.org\/site\/aboutpnas\/licenses.xhtml"}],"funder":[{"DOI":"10.13039\/501100000024","name":"Gouvernement du Canada | Canadian Institutes of Health Research","doi-asserted-by":"publisher","award":["119608"],"award-info":[{"award-number":["119608"]}],"id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002428","name":"Austrian Science Fund","doi-asserted-by":"publisher","award":["T855"],"award-info":[{"award-number":["T855"]}],"id":[{"id":"10.13039\/501100002428","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002428","name":"Austrian Science Fund","doi-asserted-by":"publisher","award":["P27031"],"award-info":[{"award-number":["P27031"]}],"id":[{"id":"10.13039\/501100002428","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2017,11,7]]},"abstract":"<jats:title>Significance<\/jats:title>\n                  <jats:p>\n                    Skeletal muscle contraction is a tightly orchestrated event that starts with the depolarization of the T-tubular membrane. At the center is a functional and mechanical coupling between two membrane proteins: L-type voltage-gated calcium channels, located in the plasma membrane, and ryanodine receptors, located in the membrane of the sarcoplasmic reticulum. How exactly these proteins associate has remained a mystery, but recent reports have highlighted a key role for the STAC3 adaptor protein in this process. Here, we provide structural snapshots of the three STAC isoforms and identify a cytosolic loop of two Ca\n                    <jats:sub>V<\/jats:sub>\n                    isoforms as a functional interaction site. A mutation linked to Native American myopathy is at the interface and abolishes the interaction.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1708852114","type":"journal-article","created":{"date-parts":[[2017,10,23]],"date-time":"2017-10-23T16:15:04Z","timestamp":1508775304000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":67,"title":["Structural insights into binding of STAC proteins to voltage-gated calcium channels"],"prefix":"10.1073","volume":"114","author":[{"given":"Siobhan M.","family":"Wong King Yuen","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of British Columbia, V6T 1Z3 Vancouver, BC, Canada;"},{"name":"The Life Sciences Centre, University of British Columbia, V6T 1Z3 Vancouver, BC, Canada;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marta","family":"Campiglio","sequence":"additional","affiliation":[{"name":"Department of Physiology and Medical Physics, Medical University of Innsbruck, 6020 Innsbruck, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ching-Chieh","family":"Tung","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of British Columbia, V6T 1Z3 Vancouver, BC, Canada;"},{"name":"The Life Sciences Centre, University of British Columbia, V6T 1Z3 Vancouver, BC, Canada;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5255-4705","authenticated-orcid":false,"given":"Bernhard E.","family":"Flucher","sequence":"additional","affiliation":[{"name":"Department of Physiology and Medical Physics, Medical University of Innsbruck, 6020 Innsbruck, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2728-8537","authenticated-orcid":false,"given":"Filip","family":"Van Petegem","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of British Columbia, V6T 1Z3 Vancouver, BC, Canada;"},{"name":"The Life Sciences Centre, University of British Columbia, V6T 1Z3 Vancouver, BC, Canada;"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2017,10,23]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"821","DOI":"10.1124\/pr.114.009654","article-title":"The physiology, pathology, and pharmacology of voltage-gated calcium channels and their future therapeutic potential","volume":"67","author":"Zamponi GW","year":"2015","unstructured":"GW Zamponi, J Striessnig, A Koschak, AC Dolphin, The physiology, pathology, and pharmacology of voltage-gated calcium channels and their future therapeutic potential. Pharmacol Rev 67, 821\u2013870 (2015).","journal-title":"Pharmacol Rev"},{"key":"e_1_3_4_2_2","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.jmb.2014.08.004","article-title":"Ryanodine receptors: Allosteric ion channel giants","volume":"427","author":"Van Petegem F","year":"2015","unstructured":"F Van Petegem, Ryanodine receptors: Allosteric ion channel giants. J Mol Biol 427, 31\u201353 (2015).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_3_2","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1038\/325717a0","article-title":"Involvement of dihydropyridine receptors in excitation-contraction coupling in skeletal muscle","volume":"325","author":"Rios E","year":"1987","unstructured":"E Rios, G Brum, Involvement of dihydropyridine receptors in excitation-contraction coupling in skeletal muscle. Nature 325, 717\u2013720 (1987).","journal-title":"Nature"},{"key":"e_1_3_4_4_2","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1038\/336134a0","article-title":"Restoration of excitation-contraction coupling and slow calcium current in dysgenic muscle by dihydropyridine receptor complementary DNA","volume":"336","author":"Tanabe T","year":"1988","unstructured":"T Tanabe, KG Beam, JA Powell, S Numa, Restoration of excitation-contraction coupling and slow calcium current in dysgenic muscle by dihydropyridine receptor complementary DNA. Nature 336, 134\u2013139 (1988).","journal-title":"Nature"},{"key":"e_1_3_4_5_2","doi-asserted-by":"crossref","first-page":"2587","DOI":"10.1083\/jcb.107.6.2587","article-title":"Structural evidence for direct interaction between the molecular components of the transverse tubule\/sarcoplasmic reticulum junction in skeletal muscle","volume":"107","author":"Block BA","year":"1988","unstructured":"BA Block, T Imagawa, KP Campbell, C Franzini-Armstrong, Structural evidence for direct interaction between the molecular components of the transverse tubule\/sarcoplasmic reticulum junction in skeletal muscle. J Cell Biol 107, 2587\u20132600 (1988).","journal-title":"J Cell Biol"},{"key":"e_1_3_4_6_2","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1038\/346569a0","article-title":"Intramembrane charge movement restored in dysgenic skeletal muscle by injection of dihydropyridine receptor cDNAs","volume":"346","author":"Adams BA","year":"1990","unstructured":"BA Adams, T Tanabe, A Mikami, S Numa, KG Beam, Intramembrane charge movement restored in dysgenic skeletal muscle by injection of dihydropyridine receptor cDNAs. Nature 346, 569\u2013572 (1990).","journal-title":"Nature"},{"key":"e_1_3_4_7_2","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1016\/S0006-3495(94)80539-9","article-title":"Restoration of junctional tetrads in dysgenic myotubes by dihydropyridine receptor cDNA","volume":"67","author":"Takekura H","year":"1994","unstructured":"H Takekura, L Bennett, T Tanabe, KG Beam, C Franzini-Armstrong, Restoration of junctional tetrads in dysgenic myotubes by dihydropyridine receptor cDNA. Biophys J 67, 793\u2013803 (1994).","journal-title":"Biophys J"},{"key":"e_1_3_4_8_2","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1038\/380072a0","article-title":"Enhanced dihydropyridine receptor channel activity in the presence of ryanodine receptor","volume":"380","author":"Nakai J","year":"1996","unstructured":"J Nakai, , Enhanced dihydropyridine receptor channel activity in the presence of ryanodine receptor. Nature 380, 72\u201375 (1996).","journal-title":"Nature"},{"key":"e_1_3_4_9_2","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1085\/jgp.115.4.467","article-title":"Functional impact of the ryanodine receptor on the skeletal muscle L-type Ca(2+) channel","volume":"115","author":"Avila G","year":"2000","unstructured":"G Avila, RT Dirksen, Functional impact of the ryanodine receptor on the skeletal muscle L-type Ca(2+) channel. J Gen Physiol 115, 467\u2013480 (2000).","journal-title":"J Gen Physiol"},{"key":"e_1_3_4_10_2","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1111\/j.1749-6632.1998.tb08253.x","article-title":"Comparative ultrastructure of Ca2+ release units in skeletal and cardiac muscle","volume":"853","author":"Franzini-Armstrong C","year":"1998","unstructured":"C Franzini-Armstrong, F Protasi, V Ramesh, Comparative ultrastructure of Ca2+ release units in skeletal and cardiac muscle. Ann N Y Acad Sci 853, 20\u201330 (1998).","journal-title":"Ann N Y Acad Sci"},{"key":"e_1_3_4_11_2","doi-asserted-by":"crossref","first-page":"43936","DOI":"10.1074\/jbc.M112.361311","article-title":"Stac3 is required for myotube formation and myogenic differentiation in vertebrate skeletal muscle","volume":"287","author":"Bower NI","year":"2012","unstructured":"NI Bower, , Stac3 is required for myotube formation and myogenic differentiation in vertebrate skeletal muscle. J Biol Chem 287, 43936\u201343949 (2012).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_12_2","doi-asserted-by":"crossref","first-page":"e62760","DOI":"10.1371\/journal.pone.0062760","article-title":"Stac3 is a novel regulator of skeletal muscle development in mice","volume":"8","author":"Reinholt BM","year":"2013","unstructured":"BM Reinholt, X Ge, X Cong, DE Gerrard, H Jiang, Stac3 is a novel regulator of skeletal muscle development in mice. PLoS One 8, e62760 (2013).","journal-title":"PLoS One"},{"key":"e_1_3_4_13_2","doi-asserted-by":"crossref","first-page":"11881","DOI":"10.1073\/pnas.1310571110","article-title":"Skeletal muscle-specific T-tubule protein STAC3 mediates voltage-induced Ca2+ release and contractility","volume":"110","author":"Nelson BR","year":"2013","unstructured":"BR Nelson, , Skeletal muscle-specific T-tubule protein STAC3 mediates voltage-induced Ca2+ release and contractility. Proc Natl Acad Sci USA 110, 11881\u201311886 (2013).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_14_2","doi-asserted-by":"crossref","first-page":"1952","DOI":"10.1038\/ncomms2952","article-title":"Stac3 is a component of the excitation-contraction coupling machinery and mutated in native American myopathy","volume":"4","author":"Horstick EJ","year":"2013","unstructured":"EJ Horstick, , Stac3 is a component of the excitation-contraction coupling machinery and mutated in native American myopathy. Nat Commun 4, 1952 (2013).","journal-title":"Nat Commun"},{"key":"e_1_3_4_15_2","doi-asserted-by":"crossref","first-page":"602","DOI":"10.1073\/pnas.1423113112","article-title":"Stac adaptor proteins regulate trafficking and function of muscle and neuronal L-type Ca2+ channels","volume":"112","author":"Polster A","year":"2015","unstructured":"A Polster, S Perni, H Bichraoui, KG Beam, Stac adaptor proteins regulate trafficking and function of muscle and neuronal L-type Ca2+ channels. Proc Natl Acad Sci USA 112, 602\u2013606 (2015).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_16_2","doi-asserted-by":"crossref","first-page":"10986","DOI":"10.1073\/pnas.1612441113","article-title":"Stac3 has a direct role in skeletal muscle-type excitation-contraction coupling that is disrupted by a myopathy-causing mutation","volume":"113","author":"Polster A","year":"2016","unstructured":"A Polster, BR Nelson, EN Olson, KG Beam, Stac3 has a direct role in skeletal muscle-type excitation-contraction coupling that is disrupted by a myopathy-causing mutation. Proc Natl Acad Sci USA 113, 10986\u201310991 (2016).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_17_2","doi-asserted-by":"crossref","first-page":"E228","DOI":"10.1073\/pnas.1619238114","article-title":"Congenital myopathy results from misregulation of a muscle Ca2+ channel by mutant Stac3","volume":"114","author":"Linsley JW","year":"2017","unstructured":"JW Linsley, , Congenital myopathy results from misregulation of a muscle Ca2+ channel by mutant Stac3. Proc Natl Acad Sci USA 114, E228\u2013E236 (2017).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_18_2","doi-asserted-by":"crossref","first-page":"41003","DOI":"10.1038\/srep41003","article-title":"STAC3 stably interacts through its C1 domain with CaV1.1 in skeletal muscle triads","volume":"7","author":"Campiglio M","year":"2017","unstructured":"M Campiglio, BE Flucher, STAC3 stably interacts through its C1 domain with CaV1.1 in skeletal muscle triads. Sci Rep 7, 41003 (2017).","journal-title":"Sci Rep"},{"key":"e_1_3_4_19_2","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1007\/s12551-012-0081-z","article-title":"SH3 domains: Modules of protein-protein interactions","volume":"5","author":"Kurochkina N","year":"2013","unstructured":"N Kurochkina, U Guha, SH3 domains: Modules of protein-protein interactions. Biophys Rev 5, 29\u201339 (2013).","journal-title":"Biophys Rev"},{"key":"e_1_3_4_20_2","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1038\/346567a0","article-title":"Regions of the skeletal muscle dihydropyridine receptor critical for excitation-contraction coupling","volume":"346","author":"Tanabe T","year":"1990","unstructured":"T Tanabe, KG Beam, BA Adams, T Niidome, S Numa, Regions of the skeletal muscle dihydropyridine receptor critical for excitation-contraction coupling. Nature 346, 567\u2013569 (1990).","journal-title":"Nature"},{"key":"e_1_3_4_21_2","doi-asserted-by":"crossref","first-page":"24983","DOI":"10.1074\/jbc.273.39.24983","article-title":"Localization in the II-III loop of the dihydropyridine receptor of a sequence critical for excitation-contraction coupling","volume":"273","author":"Nakai J","year":"1998","unstructured":"J Nakai, T Tanabe, T Konno, B Adams, KG Beam, Localization in the II-III loop of the dihydropyridine receptor of a sequence critical for excitation-contraction coupling. J Biol Chem 273, 24983\u201324986 (1998).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_22_2","doi-asserted-by":"crossref","first-page":"4721","DOI":"10.1074\/jbc.M307538200","article-title":"Structural requirements of the dihydropyridine receptor alpha1S II-III loop for skeletal-type excitation-contraction coupling","volume":"279","author":"Kugler G","year":"2004","unstructured":"G Kugler, RG Weiss, BE Flucher, M Grabner, Structural requirements of the dihydropyridine receptor alpha1S II-III loop for skeletal-type excitation-contraction coupling. J Biol Chem 279, 4721\u20134728 (2004).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_23_2","doi-asserted-by":"crossref","first-page":"D294","DOI":"10.1093\/nar\/gkv1291","article-title":"ELM 2016\u2013Data update and new functionality of the eukaryotic linear motif resource","volume":"44","author":"Dinkel H","year":"2016","unstructured":"H Dinkel, , ELM 2016\u2013Data update and new functionality of the eukaryotic linear motif resource. Nucleic Acids Res 44, D294\u2013D300 (2016).","journal-title":"Nucleic Acids Res"},{"key":"e_1_3_4_24_2","doi-asserted-by":"crossref","first-page":"5892","DOI":"10.1073\/pnas.101618098","article-title":"Excitation-contraction coupling is unaffected by drastic alteration of the sequence surrounding residues L720-L764 of the alpha 1S II-III loop","volume":"98","author":"Wilkens CM","year":"2001","unstructured":"CM Wilkens, N Kasielke, BE Flucher, KG Beam, M Grabner, Excitation-contraction coupling is unaffected by drastic alteration of the sequence surrounding residues L720-L764 of the alpha 1S II-III loop. Proc Natl Acad Sci USA 98, 5892\u20135897 (2001).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_25_2","doi-asserted-by":"crossref","first-page":"5397","DOI":"10.1038\/ncomms6397","article-title":"Crystal structures of wild type and disease mutant forms of the ryanodine receptor SPRY2 domain","volume":"5","author":"Lau K","year":"2014","unstructured":"K Lau, F Van Petegem, Crystal structures of wild type and disease mutant forms of the ryanodine receptor SPRY2 domain. Nat Commun 5, 5397 (2014).","journal-title":"Nat Commun"},{"key":"e_1_3_4_26_2","doi-asserted-by":"crossref","first-page":"1832","DOI":"10.1002\/ajmg.a.32370","article-title":"Native American myopathy: Congenital myopathy with cleft palate, skeletal anomalies, and susceptibility to malignant hyperthermia","volume":"146","author":"Stamm DS","year":"2008","unstructured":"DS Stamm, , Native American myopathy: Congenital myopathy with cleft palate, skeletal anomalies, and susceptibility to malignant hyperthermia. Am J Med Genet A 146A, 1832\u20131841 (2008).","journal-title":"Am J Med Genet A"},{"key":"e_1_3_4_27_2","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1242\/jeb.124123","article-title":"Bridging the myoplasmic gap II: More recent advances in skeletal muscle excitation-contraction coupling","volume":"219","author":"Bannister RA","year":"2016","unstructured":"RA Bannister, Bridging the myoplasmic gap II: More recent advances in skeletal muscle excitation-contraction coupling. J Exp Biol 219, 175\u2013182 (2016).","journal-title":"J Exp Biol"},{"key":"e_1_3_4_28_2","doi-asserted-by":"crossref","first-page":"21913","DOI":"10.1074\/jbc.274.31.21913","article-title":"The II-III loop of the skeletal muscle dihydropyridine receptor is responsible for the bi-directional coupling with the ryanodine receptor","volume":"274","author":"Grabner M","year":"1999","unstructured":"M Grabner, RT Dirksen, N Suda, KG Beam, The II-III loop of the skeletal muscle dihydropyridine receptor is responsible for the bi-directional coupling with the ryanodine receptor. J Biol Chem 274, 21913\u201321919 (1999).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_29_2","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1085\/jgp.200910241","article-title":"Effects of inserting fluorescent proteins into the alpha1S II-III loop: Insights into excitation-contraction coupling","volume":"134","author":"Bannister RA","year":"2009","unstructured":"RA Bannister, S Papadopoulos, CS Haarmann, KG Beam, Effects of inserting fluorescent proteins into the alpha1S II-III loop: Insights into excitation-contraction coupling. J Gen Physiol 134, 35\u201351 (2009).","journal-title":"J Gen Physiol"},{"key":"e_1_3_4_30_2","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1038\/nature02588","article-title":"Structure of a complex between a voltage-gated calcium channel beta-subunit and an alpha-subunit domain","volume":"429","author":"Van Petegem F","year":"2004","unstructured":"F Van Petegem, KA Clark, FC Chatelain, Jr DL Minor, Structure of a complex between a voltage-gated calcium channel beta-subunit and an alpha-subunit domain. Nature 429, 671\u2013675 (2004).","journal-title":"Nature"},{"key":"e_1_3_4_31_2","doi-asserted-by":"crossref","first-page":"1903","DOI":"10.1073\/pnas.95.4.1903","article-title":"Tagging with green fluorescent protein reveals a distinct subcellular distribution of L-type and non-L-type Ca2+ channels expressed in dysgenic myotubes","volume":"95","author":"Grabner M","year":"1998","unstructured":"M Grabner, RT Dirksen, KG Beam, Tagging with green fluorescent protein reveals a distinct subcellular distribution of L-type and non-L-type Ca2+ channels expressed in dysgenic myotubes. Proc Natl Acad Sci USA 95, 1903\u20131908 (1998).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_32_2","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"Xds","volume":"66","author":"Kabsch W","year":"2010","unstructured":"W Kabsch, Xds. Acta Crystallogr D Biol Crystallogr 66, 125\u2013132 (2010).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_33_2","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: A comprehensive Python-based system for macromolecular structure solution","volume":"66","author":"Adams PD","year":"2010","unstructured":"PD Adams, , PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66, 213\u2013221 (2010).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_34_2","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1107\/S0021889807021206","article-title":"Phaser crystallographic software","volume":"40","author":"McCoy AJ","year":"2007","unstructured":"AJ McCoy, , Phaser crystallographic software. J Appl Cryst 40, 658\u2013674 (2007).","journal-title":"J Appl Cryst"},{"key":"e_1_3_4_35_2","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of coot","volume":"66","author":"Emsley P","year":"2010","unstructured":"P Emsley, B Lohkamp, WG Scott, K Cowtan, Features and development of coot. Acta Crystallogr D Biol Crystallogr 66, 486\u2013501 (2010).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_36_2","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1107\/S0907444911001314","article-title":"REFMAC5 for the refinement of macromolecular crystal structures","volume":"67","author":"Murshudov GN","year":"2011","unstructured":"GN Murshudov, , REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr D Biol Crystallogr 67, 355\u2013367 (2011).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_37_2","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1083\/jcb.134.2.375","article-title":"Formation of triads without the dihydropyridine receptor alpha subunits in cell lines from dysgenic skeletal muscle","volume":"134","author":"Powell JA","year":"1996","unstructured":"JA Powell, L Petherbridge, BE Flucher, Formation of triads without the dihydropyridine receptor alpha subunits in cell lines from dysgenic skeletal muscle. J Cell Biol 134, 375\u2013387 (1996).","journal-title":"J Cell Biol"},{"key":"e_1_3_4_38_2","doi-asserted-by":"crossref","first-page":"2157","DOI":"10.1073\/pnas.0710501105","article-title":"The Timothy syndrome mutation differentially affects voltage- and calcium-dependent inactivation of CaV1.2 L-type calcium channels","volume":"105","author":"Barrett CF","year":"2008","unstructured":"CF Barrett, RW Tsien, The Timothy syndrome mutation differentially affects voltage- and calcium-dependent inactivation of CaV1.2 L-type calcium channels. Proc Natl Acad Sci USA 105, 2157\u20132162 (2008).","journal-title":"Proc Natl Acad Sci USA"}],"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.pnas.org\/syndication\/doi\/10.1073\/pnas.1708852114","content-type":"unspecified","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.1708852114","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,6,7]],"date-time":"2022-06-07T12:27:44Z","timestamp":1654604864000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.1708852114"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,10,23]]},"references-count":38,"journal-issue":{"issue":"45","published-print":{"date-parts":[[2017,11,7]]}},"alternative-id":["10.1073\/pnas.1708852114"],"URL":"https:\/\/doi.org\/10.1073\/pnas.1708852114","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[2017,10,23]]},"assertion":[{"value":"2017-10-23","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}