H. Jungbluth, C. Wallgren-pettersson, and J. Laporte, Centronuclear (myotubular) myopathy, Orphanet Journal of Rare Diseases, vol.3, issue.1, p.26, 2008.
DOI : 10.1186/1750-1172-3-26
URL : https://hal.archives-ouvertes.fr/inserm-00350775

N. Romero and M. Bitoun, Centronuclear Myopathies, Seminars in Pediatric Neurology, vol.18, issue.4, pp.250-256, 2011.
DOI : 10.1016/j.spen.2011.10.006

J. Laporte, L. Hu, C. Kretz, J. Mandel, and P. Kioschis, A gene mutated in X???linked myotubular myopathy defines a new putative tyrosine phosphatase family conserved in yeast, Nature Genetics, vol.269, issue.2, pp.175-182, 1996.
DOI : 10.1146/annurev.physiol.53.1.201

M. Bitoun, S. Maugenre, P. Jeannet, E. Lacene, and X. Ferrer, Mutations in dynamin 2 cause dominant centronuclear myopathy, Nature Genetics, vol.111, issue.11, pp.1207-1209, 2005.
DOI : 10.1083/jcb.100.1.35
URL : https://hal.archives-ouvertes.fr/hal-00187451

H. Jungbluth, H. Zhou, C. Sewry, S. Robb, and S. Treves, Centronuclear myopathy due to a de novo dominant mutation in the skeletal muscle ryanodine receptor (RYR1) gene, Neuromuscular Disorders, vol.17, issue.4, pp.338-345, 2007.
DOI : 10.1016/j.nmd.2007.01.016
URL : https://hal.archives-ouvertes.fr/hal-00189980

A. Nicot, A. Toussaint, V. Tosch, C. Kretz, and C. Wallgren-pettersson, Mutations in amphiphysin 2 (BIN1) disrupt interaction with dynamin 2 and cause autosomal recessive centronuclear myopathy, Nature Genetics, vol.18, issue.9, pp.1134-1139, 2007.
DOI : 10.1093/nar/16.1.369
URL : https://hal.archives-ouvertes.fr/hal-00189145

V. Tosch, H. Rohde, H. Tronchere, E. Zanoteli, and N. Monroy, A novel PtdIns3P and PtdIns(3,5)P2 phosphatase with an inactivating variant in centronuclear myopathy, Human Molecular Genetics, vol.15, issue.21, pp.3098-3106, 2006.
DOI : 10.1093/hmg/ddl250
URL : https://hal.archives-ouvertes.fr/hal-00188169

J. Wilmshurst, S. Lillis, H. Zhou, K. Pillay, and H. Henderson, RYR1 mutations are a common cause of congenital myopathies with central nuclei, Annals of Neurology, vol.11, issue.Spec No 2, pp.717-726, 2010.
DOI : 10.1002/ana.22119

J. Bevilacqua, N. Monnier, M. Bitoun, B. Eymard, and A. Ferreiro, Recessive RYR1 mutations cause unusual congenital myopathy with prominent nuclear internalization and large areas of myofibrillar disorganization, Neuropathology and Applied Neurobiology, vol.19, issue.3, pp.271-284, 2011.
DOI : 10.1111/j.1365-2990.2010.01149.x
URL : https://hal.archives-ouvertes.fr/inserm-00639292

S. Blot, L. Tiret, A. Devillaire, M. Fardeau, and P. Dreyfus, Phenotypic description of a canine centronuclear myopathy, J Neurol Sci, vol.199, p.9, 2002.

L. Tiret, S. Blot, J. Kessler, H. Gaillot, and M. Breen, The cnm locus, a canine homologue of human autosomal forms of centronuclear myopathy, maps to chromosome???2, Human Genetics, vol.113, issue.4, pp.297-306, 2003.
DOI : 10.1007/s00439-003-0984-7

M. Pelé, L. Tiret, J. Kessler, S. Blot, and J. Panthier, SINE exonic insertion in the PTPLA gene leads to multiple splicing defects and segregates with the autosomal recessive centronuclear myopathy in dogs, Human Molecular Genetics, vol.14, issue.11, pp.1417-1427, 2005.
DOI : 10.1093/hmg/ddi151

J. Kramer, G. Hegreberg, G. Bryan, K. Meyers, and R. Ott, A muscle disorder of Labrador retrievers characterized by deficiency of type II muscle fibers, J Am Vet Med Assoc, vol.169, pp.817-820, 1976.

R. Mckerrell, J. Anderson, M. Herrtage, J. Littlewood, and A. Palmer, Generalised muscle weakness in the Labrador retriever, Veterinary Record, vol.115, issue.11, p.276, 1984.
DOI : 10.1136/vr.115.11.276

A. Watson, B. Farrow, D. Middleton, and J. Smyth, Myopathy in a Labrador retriever, Australian Veterinary Journal, vol.48, issue.2, pp.226-227, 1988.
DOI : 10.1111/j.1751-0813.1988.tb14466.x

T. Bley, C. Gaillard, T. Bilzer, K. Braund, and D. Faissler, Genetic aspects of labrador retriever myopathy, Research in Veterinary Science, vol.73, issue.3, pp.231-236, 2002.
DOI : 10.1016/S0034-5288(02)00034-6

K. Gortel, D. Houston, T. Kuiken, C. Fries, and B. Boisvert, Inherited myopathy in a litter of Labrador retrievers, Can Vet J, vol.37, pp.108-110, 1996.

N. Olby, N. Sharp, L. Anderson, L. Kunkel, and C. Bonnemann, Evaluation of the dystrophin???glycoprotein complex, ??-actinin, dysferlin and calpain 3 in an autosomal recessive muscular dystrophy in Labrador retrievers, Neuromuscular Disorders, vol.11, issue.1, pp.41-49, 2001.
DOI : 10.1016/S0960-8966(00)00166-8

R. Mckerrell and K. Braund, Hereditary Myopathy in Labrador Retrievers: A Morphologic Study, Veterinary Pathology, vol.9, issue.4, pp.411-417, 1986.
DOI : 10.1177/030098588602300410

R. Mckerrell and K. Braund, Hereditary myopathy in Labrador Retrievers: clinical variations, Journal of Small Animal Practice, vol.10, issue.1, pp.479-489, 1987.
DOI : 10.1111/j.1748-5827.1987.tb01441.x

L. Clark, J. Wahl, C. Rees, and K. Murphy, From The Cover: Retrotransposon insertion in SILV is responsible for merle patterning of the domestic dog, Proceedings of the National Academy of Sciences, vol.103, issue.5, pp.1376-1381, 2006.
DOI : 10.1073/pnas.0506940103

Y. Xue, Q. Wang, Q. Long, B. Ng, and H. Swerdlow, Human Y Chromosome Base-Substitution Mutation Rate Measured by Direct Sequencing in a Deep-Rooting Pedigree, Current Biology, vol.19, issue.17, pp.1453-1457, 2009.
DOI : 10.1016/j.cub.2009.07.032

M. Owczarek-lipska, A. Thomas, C. Andre, S. Holzer, and T. Leeb, H??ufigkeit von Gendefekten in ausgew??hlten europ??ischen Retriever-Populationen, Schweizer Archiv f??r Tierheilkunde, vol.153, issue.9, pp.418-420, 2011.
DOI : 10.1024/0036-7281/a000236

K. Lindblad-toh, C. Wade, T. Mikkelsen, E. Karlsson, and D. Jaffe, Genome sequence, comparative analysis and haplotype structure of the domestic dog, Nature, vol.426, issue.7069, pp.803-819, 2005.
DOI : 10.1038/nature04338

M. Knapp, Retriver Field Trials The Official Book of the Labarador Retriever, pp.181-204, 1995.

J. Dowling, E. Gibbs, and E. Feldman, Membrane Traffic and Muscle: Lessons from Human Disease, Traffic, vol.74, issue.7, pp.1035-1043, 2008.
DOI : 10.1016/j.nmd.2007.06.467

B. Cowling, A. Toussaint, J. Muller, and J. Laporte, Defective Membrane Remodeling in Neuromuscular Diseases: Insights from Animal Models, PLoS Genetics, vol.283, issue.4, p.1002595, 2012.
DOI : 10.1371/journal.pgen.1002595.s003

A. Toussaint, B. Cowling, K. Hnia, M. Mohr, and A. Oldfors, Defects in amphiphysin 2 (BIN1) and triads in several forms of centronuclear myopathies, Acta Neuropathologica, vol.18, issue.2, pp.253-266, 2011.
DOI : 10.1007/s00401-010-0754-2

K. Hnia, H. Tronchere, K. Tomczak, L. Amoasii, and P. Schultz, Myotubularin controls desmin intermediate filament architecture and mitochondrial dynamics in human and mouse skeletal muscle, Journal of Clinical Investigation, vol.121, issue.1, pp.70-85, 2011.
DOI : 10.1172/JCI44021DS1

A. Razzaq, I. Robinson, H. Mcmahon, J. Skepper, and Y. Su, Amphiphysin is necessary for organization of the excitation-contraction coupling machinery of muscles, but not for synaptic vesicle endocytosis in Drosophila, Genes & Development, vol.15, issue.22, pp.2967-2979, 2001.
DOI : 10.1101/gad.207801

L. Al-qusairi, N. Weiss, A. Toussaint, C. Berbey, and N. Messaddeq, T-tubule disorganization and defective excitation-contraction coupling in muscle fibers lacking myotubularin lipid phosphatase, Proceedings of the National Academy of Sciences, vol.106, issue.44, pp.18763-18768, 2009.
DOI : 10.1073/pnas.0900705106

J. Shen, W. Yu, M. Brotto, J. Scherman, and C. Guo, Deficiency of MIP/MTMR14 phosphatase induces a muscle disorder by disrupting Ca2+ homeostasis, Nature Cell Biology, vol.21, issue.6, pp.769-776, 2009.
DOI : 10.1016/S0006-3495(97)78124-4

J. Dowling, A. Vreede, S. Low, E. Gibbs, and J. Kuwada, Loss of Myotubularin Function Results in T-Tubule Disorganization in Zebrafish and Human Myotubular Myopathy, PLoS Genetics, vol.9, issue.2, p.1000372, 2009.
DOI : 10.1371/journal.pgen.1000372.s009

B. Cowling, A. Toussaint, L. Amoasii, P. Koebel, and A. Ferry, Increased Expression of Wild-Type or a Centronuclear Myopathy Mutant of Dynamin 2 in Skeletal Muscle of Adult Mice Leads to Structural Defects and Muscle Weakness, The American Journal of Pathology, vol.178, issue.5, pp.2224-2235, 2011.
DOI : 10.1016/j.ajpath.2011.01.054

F. Blondeau, J. Laporte, S. Bodin, G. Superti-furga, and B. Payrastre, Myotubularin, a phosphatase deficient in myotubular myopathy, acts on phosphatidylinositol 3-kinase and phosphatidylinositol 3-phosphate pathway, Human Molecular Genetics, vol.9, issue.15, pp.2223-2229, 2000.
DOI : 10.1093/oxfordjournals.hmg.a018913

A. Fidzianska and H. Goebel, Aberrant arrested in maturation neuromuscular junctions in centronuclear myopathy, Journal of the Neurological Sciences, vol.124, issue.1, pp.83-88, 1994.
DOI : 10.1016/0022-510X(94)90015-9

J. Dowling, R. Joubert, S. Low, A. Durban, and N. Messaddeq, Myotubular myopathy and the neuromuscular junction: a novel therapeutic approach from mouse models, Disease models & mechanisms, 2012.
DOI : 10.1242/dmm.009746

V. Denic and J. Weissman, A Molecular Caliper Mechanism for Determining Very Long-Chain Fatty Acid Length, Cell, vol.130, issue.4, pp.663-677, 2007.
DOI : 10.1016/j.cell.2007.06.031

M. Ikeda, Y. Kanao, M. Yamanaka, H. Sakuraba, and Y. Mizutani, Characterization of four mammalian 3-hydroxyacyl-CoA dehydratases involved in very long-chain fatty acid synthesis, FEBS Letters, vol.275, issue.16, pp.2435-2440, 2008.
DOI : 10.1016/j.febslet.2008.06.007

E. Posse-de-chaves and S. Sipione, Sphingolipids and gangliosides of the nervous system in membrane function and dysfunction, FEBS Letters, vol.14, issue.9, pp.1748-1759, 2010.
DOI : 10.1016/j.febslet.2009.12.010

A. Kihara, H. Sakuraba, M. Ikeda, A. Denpoh, and Y. Igarashi, Membrane Topology and Essential Amino Acid Residues of Phs1, a 3-Hydroxyacyl-CoA Dehydratase Involved in Very Long-chain Fatty Acid Elongation, Journal of Biological Chemistry, vol.283, issue.17, pp.11199-11209, 2008.
DOI : 10.1074/jbc.M708993200

A. Beggs, J. Bohm, E. Snead, M. Kozlowski, and M. Maurer, MTM1 mutation associated with X-linked myotubular myopathy in Labrador Retrievers, Proceedings of the National Academy of Sciences, vol.107, issue.33, pp.14697-14702, 2010.
DOI : 10.1073/pnas.1003677107
URL : https://hal.archives-ouvertes.fr/inserm-00511900