{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T08:46:32Z","timestamp":1792658792080,"version":"4.5.0"},"reference-count":44,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2020,11,11]],"date-time":"2020-11-11T00:00:00Z","timestamp":1605052800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2020,11,11]],"date-time":"2020-11-11T00:00:00Z","timestamp":1605052800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001677","name":"Inserm","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100001677","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100004923","name":"AFM-T\u00e9l\u00e9thon","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004923","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["acta neuropathol commun"],"published-print":{"date-parts":[[2020,12]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Mutations in the\n                    <jats:italic>RYR1<\/jats:italic>\n                    gene, encoding the skeletal muscle calcium channel RyR1, lead to congenital myopathies, through expression of a channel with abnormal permeability and\/or in reduced amount, but the direct functional whole organism consequences of exclusive reduction in RyR1 amount have never been studied. We have developed and characterized a mouse model with inducible muscle specific\n                    <jats:italic>RYR1<\/jats:italic>\n                    deletion. Tamoxifen-induced recombination in the\n                    <jats:italic>RYR1<\/jats:italic>\n                    gene at adult age resulted in a progressive reduction in the protein amount reaching a stable level of 50% of the initial amount, and was associated with a progressive muscle weakness and atrophy. Measurement of calcium fluxes in isolated muscle fibers demonstrated a reduction in the amplitude of RyR1-related calcium release mirroring the reduction in the protein amount. Alterations in the muscle structure were observed, with fibers atrophy, abnormal mitochondria distribution and membrane remodeling. An increase in the expression level of many proteins was observed, as well as an inhibition of the autophagy process. This model demonstrates that RyR1 reduction is sufficient to recapitulate most features of Central Core Disease, and accordingly similar alterations were observed in muscle biopsies from Dusty Core Disease patients (a subtype of Central Core Disease), pointing to common pathophysiological mechanisms related to RyR1 reduction.\n                  <\/jats:p>","DOI":"10.1186\/s40478-020-01068-4","type":"journal-article","created":{"date-parts":[[2020,11,11]],"date-time":"2020-11-11T07:03:19Z","timestamp":1605078199000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":28,"title":["In vivo RyR1 reduction in muscle triggers a core-like myopathy"],"prefix":"10.1186","volume":"8","author":[{"given":"Laurent","family":"Pelletier","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anne","family":"Petiot","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Julie","family":"Brocard","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Benoit","family":"Giannesini","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Diane","family":"Giovannini","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Colline","family":"Sanchez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lauriane","family":"Travard","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mathilde","family":"Chivet","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mathilde","family":"Beaufils","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Candice","family":"Kutchukian","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David","family":"Bendahan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel","family":"Metzger","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Clara","family":"Franzini Armstrong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Norma B.","family":"Romero","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John","family":"Rendu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vincent","family":"Jacquemond","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Julien","family":"Faur\u00e9","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3625-913X","authenticated-orcid":false,"given":"Isabelle","family":"Marty","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2020,11,11]]},"reference":[{"key":"1068_CR1","doi-asserted-by":"publisher","first-page":"2270","DOI":"10.1073\/pnas.91.6.2270","volume":"91","author":"I Marty","year":"1994","unstructured":"Marty I, Robert M, Villaz M, Lai Y, De Jongh KS, Catterall WA et al (1994) Biochemical evidence for a complex involving dihydropyridine receptor and ryanodine receptor in triad junctions of skeletal muscle. Proc Natl Acad Sci USA 91:2270\u20132274. https:\/\/doi.org\/10.1073\/pnas.91.6.2270","journal-title":"Proc Natl Acad Sci USA"},{"key":"1068_CR2","doi-asserted-by":"publisher","first-page":"23389","DOI":"10.1074\/jbc.272.37.23389","volume":"272","author":"L Zhang","year":"1997","unstructured":"Zhang L, Kelley J, Schmeisser G, Kobayashi YM, Jones LR (1997) Complex formation between junctin,\u00a0triadin, calsequestrin, and the\u00a0ryanodine\u00a0receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane. J Biol Chem 272:23389\u201323397. https:\/\/doi.org\/10.1074\/jbc.272.37.23389","journal-title":"J Biol Chem"},{"key":"1068_CR3","doi-asserted-by":"publisher","first-page":"189","DOI":"10.1016\/s1050-1738(02)00163-9","volume":"12","author":"RT Dirksen","year":"2002","unstructured":"Dirksen RT, Avila G (2002) Altered\u00a0ryanodine\u00a0receptor\u00a0function in central core disease: leaky or uncoupled Ca(2+)\u00a0release\u00a0channels? Trends Cardiovasc Med 12:189\u2013197. https:\/\/doi.org\/10.1016\/s1050-1738(02)00163-9","journal-title":"Trends Cardiovasc Med"},{"key":"1068_CR4","doi-asserted-by":"publisher","first-page":"467","DOI":"10.1007\/s00424-010-0794-4","volume":"460","author":"MJ Betzenhauser","year":"2010","unstructured":"Betzenhauser MJ, Marks AR (2010) Ryanodine receptor channelopathies. Pflugers Arch 460:467\u2013480. https:\/\/doi.org\/10.1007\/s00424-010-0794-4","journal-title":"Pflugers Arch"},{"key":"1068_CR5","doi-asserted-by":"publisher","first-page":"a003996","DOI":"10.1101\/cshperspect.a003996","volume":"2","author":"JT Lanner","year":"2010","unstructured":"Lanner JT, Georgiou DK, Joshi AD, Hamilton SL (2010) Ryanodine receptors: structure, expression, molecular details, and function in calcium release. Cold Spring Harb Perspect Biol 2:a003996. https:\/\/doi.org\/10.1101\/cshperspect.a003996","journal-title":"Cold Spring Harb Perspect Biol"},{"key":"1068_CR6","doi-asserted-by":"publisher","first-page":"948","DOI":"10.1016\/j.bbamcr.2010.11.009","volume":"1813","author":"DH MacLennan","year":"2011","unstructured":"MacLennan DH, Zvaritch E (2011) Mechanistic models for muscle diseases and disorders originating in the sarcoplasmic reticulum. Biochim Biophys Acta 1813:948\u2013964. https:\/\/doi.org\/10.1016\/j.bbamcr.2010.11.009","journal-title":"Biochim Biophys Acta"},{"key":"1068_CR7","doi-asserted-by":"publisher","first-page":"443","DOI":"10.3233\/JND-160172","volume":"3","author":"I Marty","year":"2016","unstructured":"Marty I, Faur\u00e9 J (2016) Excitation-contraction coupling alterations in myopathies. J Neuromusc Dis 3:443\u2013453. https:\/\/doi.org\/10.3233\/JND-160172","journal-title":"J Neuromusc Dis"},{"key":"1068_CR8","doi-asserted-by":"publisher","first-page":"151","DOI":"10.1038\/nrneurol.2017.191","volume":"14","author":"H Jungbluth","year":"2018","unstructured":"Jungbluth H, Treves S, Zorzato F, Sarkozy A, Ochala J, Sewry C et al (2018) Congenital myopathies: disorders of excitation-contraction coupling and muscle contraction. Nat Rev Neurol 14:151\u2013167. https:\/\/doi.org\/10.1038\/nrneurol.2017.191","journal-title":"Nat Rev Neurol"},{"key":"1068_CR9","doi-asserted-by":"publisher","first-page":"329","DOI":"10.1096\/fj.05-4497fje","volume":"20","author":"MG Chelu","year":"2006","unstructured":"Chelu MG, Goonasekera SA, Durham WJ, Tang W, Lueck JD, Riehl J et al (2006) Heat- and anesthesia-induced malignant hyperthermia in an\u00a0RyR1\u00a0knock-in\u00a0mouse. FASEB J 20:329\u2013330. https:\/\/doi.org\/10.1096\/fj.05-4497fje","journal-title":"FASEB J"},{"key":"1068_CR10","doi-asserted-by":"publisher","first-page":"21813","DOI":"10.1073\/pnas.0912126106","volume":"106","author":"E Zvaritch","year":"2009","unstructured":"Zvaritch E, Kraeva N, Bombardier E, McCloy RA, Depreux F, Holmyard D et al (2009) Ca2+\u2009dysregulation in\u00a0Ryr1(I4895T\/wt)\u00a0mice\u00a0causes congenital myopathy with progressive formation of minicores, cores, and nemaline rods. Proc Natl Acad Sci USA 106:21813\u201321818. https:\/\/doi.org\/10.1073\/pnas.0912126106","journal-title":"Proc Natl Acad Sci USA"},{"key":"1068_CR11","doi-asserted-by":"publisher","first-page":"3024","DOI":"10.1093\/hmg\/ddz105","volume":"28","author":"S Brennan","year":"2019","unstructured":"Brennan S, Garcia-Casta\u00f1eda M, Michelucci A, Sabha N, Malik S, Groom L et al (2019) Mouse\u00a0model\u00a0of severe recessive\u00a0RYR1-related myopathy. Hum Mol Genet 28:3024\u20133036. https:\/\/doi.org\/10.1093\/hmg\/ddz105","journal-title":"Hum Mol Genet"},{"key":"1068_CR12","doi-asserted-by":"publisher","first-page":"2987","DOI":"10.1093\/hmg\/ddz092","volume":"28","author":"M Elbaz","year":"2019","unstructured":"Elbaz M, Ruiz A, Bachmann C, Eckhardt J, Pelczar P, Venturi E, Lindsay C et al (2019) Quantitative\u00a0RyR1\u00a0reduction and loss of\u00a0calcium\u00a0sensitivity of RyR1Q1970fsX16\u2009+\u2009A4329D cause cores and loss of muscle strength. Hum Mol Genet 28:2987\u20132999. https:\/\/doi.org\/10.1093\/hmg\/ddz092","journal-title":"Hum Mol Genet"},{"key":"1068_CR13","doi-asserted-by":"publisher","first-page":"1872","DOI":"10.1093\/hmg\/ddz025","volume":"28","author":"M Elbaz","year":"2019","unstructured":"Elbaz M, Ruiz A, Eckhardt J, Pelczar P, Muntoni F, Boncompagni S et al (2019) Quantitative reduction of\u00a0RyR1\u00a0protein caused by a single-allele frameshift mutation in\u00a0RYR1\u00a0ex36 impairs the strength of adult skeletal muscle fibres. Hum Mol Genet 28:1872\u20131884. https:\/\/doi.org\/10.1093\/hmg\/ddz025","journal-title":"Hum Mol Genet"},{"key":"1068_CR14","doi-asserted-by":"publisher","first-page":"556","DOI":"10.1038\/369556a0","volume":"369","author":"H Takeshima","year":"1994","unstructured":"Takeshima H, Iino M, Takekura H, Nishi M, Kuno J, Minowa O et al (1994) Excitation-contraction uncoupling and muscular degeneration in mice lacking functional skeletal muscle ryanodine-receptor gene. Nature 369:556\u2013559. https:\/\/doi.org\/10.1038\/369556a0","journal-title":"Nature"},{"key":"1068_CR15","doi-asserted-by":"publisher","first-page":"421","DOI":"10.3233\/JND-150073","volume":"2","author":"M Cacheux","year":"2015","unstructured":"Cacheux M, Blum A, S\u00e9bastien M, Wozny AS, Brocard J, Mamchaoui K et al (2015) Functional characterization of a Central Core Disease RyR1 mutation (p. Y4864H) associated with quantitative defect in RyR1 protein. J. Neuromusc Dis 2:421\u2013432. https:\/\/doi.org\/10.3233\/JND-150073","journal-title":"J. Neuromusc Dis"},{"key":"1068_CR16","doi-asserted-by":"publisher","first-page":"3","DOI":"10.1186\/s40478-018-0655-5","volume":"7","author":"M Garibaldi","year":"2019","unstructured":"Garibaldi M, Rendu J, Brocard J, Lacene E, Faur\u00e9 J, Brochier G et al (2019) \u2018Dusty core disease\u2019 (DuCD): expanding morphological spectrum of RYR1 recessive myopathies. Acta Neuropathol Commun 7:3. https:\/\/doi.org\/10.1186\/s40478-018-0655-5","journal-title":"Acta Neuropathol Commun"},{"key":"1068_CR17","doi-asserted-by":"publisher","first-page":"165","DOI":"10.1002\/gene.20107","volume":"41","author":"M Schuler","year":"2005","unstructured":"Schuler M, Ali F, Metzger E, Chambon P, Metzger D (2005) Temporally controlled targeted somatic mutagenesis in skeletal muscles of the\u00a0mouse. Genesis 41:165\u2013170. https:\/\/doi.org\/10.1002\/gene.20107","journal-title":"Genesis"},{"key":"1068_CR18","doi-asserted-by":"publisher","first-page":"8206","DOI":"10.1074\/jbc.275.11.8206","volume":"275","author":"I Marty","year":"2000","unstructured":"Marty I, Thevenon D, Scotto C, Groh S, Sainnier S, Robert M et al (2000) Cloning and characterization of a new isoform of skeletal muscle triadin. J Biol Chem 275:8206\u20138212. https:\/\/doi.org\/10.1074\/jbc.275.11.8206","journal-title":"J Biol Chem"},{"key":"1068_CR19","doi-asserted-by":"publisher","first-page":"3744","DOI":"10.1242\/jcs.188862","volume":"129","author":"A Osseni","year":"2016","unstructured":"Osseni A, S\u00e9bastien M, Sarrault O, Baudet M, Cout\u00e9 Y, Faur\u00e9 J et al (2016) Triadin and CLIMP-63 form a link between triads and microtubules in muscle cells. J Cell Sci 129:3744\u20133755. https:\/\/doi.org\/10.1242\/jcs.188862","journal-title":"J Cell Sci"},{"key":"1068_CR20","doi-asserted-by":"crossref","first-page":"11147","DOI":"10.1016\/S0021-9258(19)78103-4","volume":"269","author":"MJ Moutin","year":"1994","unstructured":"Moutin MJ, Cuillel M, Rapin C, Miras R, Anger M, Lompr\u00e9 AM et al (1994) Measurements of ATP binding on the large cytoplasmic loop of the sarcoplasmic reticulum Ca(2+)-ATPase overexpressed in Escherichia coli. J Biol Chem 269:11147\u201311154","journal-title":"J Biol Chem"},{"key":"1068_CR21","doi-asserted-by":"publisher","first-page":"223","DOI":"10.1016\/0014-5793(89)80226-1","volume":"245","author":"J Lunardi","year":"1989","unstructured":"Lunardi J, Dupuis A, Frobert Y, Grassi J, Vignais PV (1989) Exploration of delta-subunit interactions in beef heart mitochondrial F1-ATPase by monoclonal antibodies. FEBS Lett 245:223\u2013228. https:\/\/doi.org\/10.1016\/0014-5793(89)80226-1","journal-title":"FEBS Lett"},{"key":"1068_CR22","doi-asserted-by":"publisher","first-page":"34918","DOI":"10.1074\/jbc.M109.022442","volume":"284","author":"S Oddoux","year":"2009","unstructured":"Oddoux S, Brocard J, Schweitzer A, Szentesi P, Giannesini B, Brocard J et al (2009) Triadin deletion induces impaired skeletal muscle function. J Biol Chem 284:34918\u201334929. https:\/\/doi.org\/10.1074\/jbc.M109.022442","journal-title":"J Biol Chem"},{"key":"1068_CR23","doi-asserted-by":"publisher","first-page":"262","DOI":"10.1002\/mrm.22386","volume":"64","author":"B Giannesini","year":"2010","unstructured":"Giannesini B, Vilmen C, Le Fur Y, Dalmasso C, Cozzone PJ, Bendahan D (2010) A strictly noninvasive MR setup dedicated to longitudinal studies of mechanical performance, bioenergetics, anatomy, and muscle recruitment in contracting mouse skeletal muscle. Magn Reson Med 64:262\u2013270. https:\/\/doi.org\/10.1002\/mrm.22386","journal-title":"Magn Reson Med"},{"key":"1068_CR24","doi-asserted-by":"publisher","first-page":"159","DOI":"10.1007\/978-1-4939-1096-0_9","volume":"1183","author":"R Lefebvre","year":"2014","unstructured":"Lefebvre R, Pouvreau S, Collet C, Allard B, Jacquemond V (2014) Whole-cell voltage clamp on skeletal muscle fibers with the silicone-clamp technique. Methods Mol Biol 1183:159\u2013170. https:\/\/doi.org\/10.1007\/978-1-4939-1096-0_9","journal-title":"Methods Mol Biol"},{"key":"1068_CR25","doi-asserted-by":"publisher","first-page":"14432","DOI":"10.1073\/pnas.1604099113","volume":"113","author":"C Kutchukian","year":"2016","unstructured":"Kutchukian C, Lo Scrudato M, Tourneur Y, Poulard K, Vignaud A, Berthier C et al (2016) Phosphatidylinositol 3-kinase inhibition restores Ca2+\u2009release defects and prolongs survival in myotubularin-deficient mice. Proc Natl Acad Sci USA 113:14432\u201314437. https:\/\/doi.org\/10.1073\/pnas.1604099113","journal-title":"Proc Natl Acad Sci USA"},{"key":"1068_CR26","doi-asserted-by":"publisher","first-page":"7369","DOI":"10.1113\/JP274990","volume":"595","author":"C Kutchukian","year":"2017","unstructured":"Kutchukian C, Szentesi P, Allard B, Trochet D, Beuvin M, Berthier C et al (2017) Impaired excitation-contraction coupling in muscle fibres from the dynamin2R465W\u00a0mouse model of centronuclear myopathy. J Physiol 595:7369\u20137382. https:\/\/doi.org\/10.1113\/JP274990","journal-title":"J Physiol"},{"key":"1068_CR27","doi-asserted-by":"publisher","first-page":"581","DOI":"10.1042\/cs0890581","volume":"89","author":"GJ Kemp","year":"1995","unstructured":"Kemp GJ, Hands LJ, Ramaswami G, Taylor DJ, Nicolaides A, Amato A et al (1995) Calf muscle mitochondrial and glycogenolytic ATP synthesis in patients with claudication due to peripheral vascular disease analysed using 31P magnetic resonance spectroscopy. Clin Sci (Lond) 89:581\u2013590. https:\/\/doi.org\/10.1042\/cs0890581","journal-title":"Clin Sci (Lond)"},{"key":"1068_CR28","doi-asserted-by":"publisher","first-page":"767","DOI":"10.1113\/jphysiol.2007.138024","volume":"583","author":"C Paolini","year":"2007","unstructured":"Paolini C, Quarta M, Nori A, Boncompagni S, Canato M, Volpe P et al (2007) Reorganized stores and impaired calcium handling in skeletal muscle of mice lacking calsequestrin-1. J Physiol 583:767\u2013784. https:\/\/doi.org\/10.1113\/jphysiol.2007.138024","journal-title":"J Physiol"},{"key":"1068_CR29","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1016\/j.ab.2012.10.010","volume":"433","author":"A G\u00fcrtler","year":"2013","unstructured":"G\u00fcrtler A, Kunz N, Gomolka M, Hornhardt S, Friedl AA, McDonald K et al (2013) Stain-free technology as a normalization tool in Western blot analysis. Anal Biochem 433:105\u2013111. https:\/\/doi.org\/10.1016\/j.ab.2012.10.010","journal-title":"Anal Biochem"},{"key":"1068_CR30","doi-asserted-by":"publisher","first-page":"869","DOI":"10.1111\/j.1600-0854.2012.01348.x","volume":"13","author":"AC Durieux","year":"2012","unstructured":"Durieux AC, Vassilopoulos S, Lain\u00e9 J, Fraysse B, Bri\u00f1as L, Prudhon B et al (2012) A centronuclear myopathy-dynamin 2 mutation impairs autophagy in mice. Traffic 13:869\u2013879. https:\/\/doi.org\/10.1111\/j.1600-0854.2012.01348.x","journal-title":"Traffic"},{"key":"1068_CR31","doi-asserted-by":"publisher","first-page":"3384","DOI":"10.1096\/fj.12-220947","volume":"27","author":"L Al-Qusairi","year":"2013","unstructured":"Al-Qusairi L, Prokic I, Amoasii L, Kretz C, Messaddeq N, Mandel JL et al (2013) Lack of myotubularin (MTM1) leads to muscle hypotrophy through unbalanced regulation of the autophagy and ubiquitin-proteasome pathways. FASEB J 27:3384\u20133394. https:\/\/doi.org\/10.1096\/fj.12-220947","journal-title":"FASEB J"},{"key":"1068_CR32","doi-asserted-by":"publisher","first-page":"5885","DOI":"10.1074\/jbc.273.10.5885","volume":"273","author":"DA Ferrington","year":"1998","unstructured":"Ferrington DA, Krainev AG, Bigelow DJ (1998) Altered\u00a0turnover\u00a0of calcium regulatory proteins of the sarcoplasmic reticulum in aged\u00a0skeletal muscle. J Biol Chem 273:5885\u20135891. https:\/\/doi.org\/10.1074\/jbc.273.10.5885","journal-title":"J Biol Chem"},{"key":"1068_CR33","doi-asserted-by":"publisher","first-page":"440","DOI":"10.1016\/0003-9861(72)90237-8","volume":"152","author":"A Martonosi","year":"1972","unstructured":"Martonosi A, Halpin RA (1972) Sarcoplasmic reticulum. XVII. The turnover of proteins and phospholipids in sarcoplasmic reticulum membranes. Arch Biochem Biophys 152:440\u2013450. https:\/\/doi.org\/10.1016\/0003-9861(72)90237-8","journal-title":"Arch Biochem Biophys"},{"key":"1068_CR34","doi-asserted-by":"publisher","first-page":"643","DOI":"10.1038\/emboj.2009.366","volume":"29","author":"F Pi\u00e9tri-Rouxel","year":"2010","unstructured":"Pi\u00e9tri-Rouxel F, Gentil C, Vassilopoulos S, Baas D, Mouisel E, Ferry A et al (2010) DHPR \u03b11S subunit controls skeletal muscle mass and morphogenesis. EMBO J 29:643\u2013654. https:\/\/doi.org\/10.1038\/emboj.2009.366","journal-title":"EMBO J"},{"key":"1068_CR35","doi-asserted-by":"publisher","first-page":"d659","DOI":"10.2741\/A802","volume":"7","author":"RT Dirksen","year":"2002","unstructured":"Dirksen RT (2002) Bi-directional coupling between dihydropyridine receptors and ryanodine receptors. Front Biosci 7:d659\u2013d670","journal-title":"Front Biosci"},{"key":"1068_CR36","doi-asserted-by":"publisher","first-page":"72","DOI":"10.1038\/380072a0","volume":"380","author":"J Nakai","year":"1996","unstructured":"Nakai J, Dirksen RT, Nguyen HT, Pessah IN, Beam KG, Allen PD (1996) Enhanced dihydropyridine receptor channel activity in the presence of ryanodine receptor. Nature 380:72\u201375. https:\/\/doi.org\/10.1038\/380072a0","journal-title":"Nature"},{"key":"1068_CR37","doi-asserted-by":"publisher","first-page":"2587","DOI":"10.1083\/jcb.107.6.2587","volume":"107","author":"BA Block","year":"1988","unstructured":"Block BA, Imagawa T, Campbell KP, Franzini-Armstrong C (1988) 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. https:\/\/doi.org\/10.1083\/jcb.107.6.2587","journal-title":"J Cell Biol"},{"key":"1068_CR38","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.yexcr.2004.08.004","volume":"301","author":"D Paulin","year":"2004","unstructured":"Paulin D, Li Z (2004) Desmin: a major intermediate filament protein essential for the structural integrity and function of muscle. Exp Cell Res 301:1\u20137. https:\/\/doi.org\/10.1016\/j.yexcr.2004.08.004","journal-title":"Exp Cell Res"},{"key":"1068_CR39","doi-asserted-by":"publisher","first-page":"579","DOI":"10.1091\/mbc.E18-11-0718","volume":"30","author":"A Franck","year":"2019","unstructured":"Franck A, Lain\u00e9 J, Moulay G, Lemerle E, Trichet M, Gentil C et al (2019) Clathrin plaques and associated actin anchor intermediate filaments in skeletal muscle. Mol Biol Cell 30:579\u2013590. https:\/\/doi.org\/10.1091\/mbc.E18-11-0718","journal-title":"Mol Biol Cell"},{"key":"1068_CR40","doi-asserted-by":"publisher","first-page":"1806","DOI":"10.1172\/JCI38027","volume":"119","author":"LG Goldfarb","year":"2009","unstructured":"Goldfarb LG, Dalakas MC (2009) Tragedy in a heartbeat: malfunctioning desmin causes skeletal and cardiac muscle disease. J Clin Invest 119:1806\u20131813. https:\/\/doi.org\/10.1172\/JCI38027","journal-title":"J Clin Invest"},{"key":"1068_CR41","doi-asserted-by":"publisher","first-page":"2492","DOI":"10.1016\/j.bbamcr.2013.04.009","volume":"1833","author":"U Goyal","year":"2013","unstructured":"Goyal U, Blackstone C (2013) Untangling the web: mechanisms underlying ER network formation. Biochim Biophys Acta 1833:2492\u20132498. https:\/\/doi.org\/10.1016\/j.bbamcr.2013.04.009","journal-title":"Biochim Biophys Acta"},{"key":"1068_CR42","doi-asserted-by":"publisher","first-page":"e47576","DOI":"10.7554\/eLife.47576","volume":"8","author":"A Michelucci","year":"2019","unstructured":"Michelucci A, Boncompagni S, Pietrangelo L, Garc\u00eda-Casta\u00f1eda M, Takano T, Malik S et al (2019) Transverse tubule remodeling enhances Orai1-dependent Ca2+\u00a0entry in skeletal muscle. Elife 8:e47576. https:\/\/doi.org\/10.7554\/eLife.47576","journal-title":"Elife"},{"key":"1068_CR43","doi-asserted-by":"publisher","first-page":"14286","DOI":"10.1038\/s41598-017-14134-0","volume":"7","author":"S Boncompagni","year":"2017","unstructured":"Boncompagni S, Michelucci A, Pietrangelo L, Dirksen RT, Protasi F (2017) Exercise-dependent formation of new junctions that promote STIM1-Orai1 assembly in skeletal muscle. Sci Rep 7:14286. https:\/\/doi.org\/10.1038\/s41598-017-14134-0","journal-title":"Sci Rep"},{"key":"1068_CR44","doi-asserted-by":"publisher","first-page":"507","DOI":"10.1016\/j.cmet.2009.10.008","volume":"10","author":"E Masiero","year":"2009","unstructured":"Masiero E, Agatea L, Mammucari C, Blaauw B, Loro E, Komatsu M et al (2009) Autophagy is required to maintain muscle mass. Cell Metab 10:507\u2013515. https:\/\/doi.org\/10.1016\/j.cmet.2009.10.008","journal-title":"Cell Metab"}],"container-title":["Acta Neuropathologica Communications"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1186\/s40478-020-01068-4.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/article\/10.1186\/s40478-020-01068-4\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1186\/s40478-020-01068-4.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,4,13]],"date-time":"2021-04-13T20:16:26Z","timestamp":1618344986000},"score":1,"resource":{"primary":{"URL":"https:\/\/actaneurocomms.biomedcentral.com\/articles\/10.1186\/s40478-020-01068-4"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,11,11]]},"references-count":44,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2020,12]]}},"alternative-id":["1068"],"URL":"https:\/\/doi.org\/10.1186\/s40478-020-01068-4","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/2020.08.27.269647","asserted-by":"object"}]},"ISSN":["2051-5960"],"issn-type":[{"value":"2051-5960","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,11,11]]},"assertion":[{"value":"8 September 2020","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"27 October 2020","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"11 November 2020","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"All procedures using animals were approved by the institutional ethics committee (CEEA-GIN 04, N_134) and followed the guidelines from Directive 2010\/63\/EU of the European Parliament on the protection of animals used for scientific purposes. Experimental procedures for human studies were approved by the institutional ethics committee and performed in accordance with ethical standards laid down in the Declaration of Helsinki. All biopsies were collected following informed consent.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics approval"}},{"value":"Not applicable.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent for publication"}},{"value":"The authors declare that they have no competing interests.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"192"}}