G. Wiche, Role of plectin in cytoskeleton organization and dynamics, J. Cell Sci, vol.11, pp.2477-2486, 1998.

I. Letunic, T. Doerks, and P. Bork, SMART 7: recent updates to the protein domain annotation resource, Nucleic Acids Research, vol.40, issue.D1, pp.302-305, 2011.
DOI : 10.1093/nar/gkr931

J. A. Mellad, D. T. Warren, and C. M. Shanahan, Nesprins LINC the nucleus and cytoskeleton, Current Opinion in Cell Biology, vol.23, issue.1, pp.47-54, 2011.
DOI : 10.1016/j.ceb.2010.11.006

J. G. Boyer, M. A. Bernstein, and C. Boudreau-larivière, Plakins in striated muscle, Muscle & Nerve, vol.575, issue.Pt 6, pp.299-308, 2010.
DOI : 10.1002/mus.21472

M. R. Schiller, Autonomous functions for the Sec14p/spectrin-repeat region of Kalirin, Experimental Cell Research, vol.314, issue.14, pp.2674-2691, 2008.
DOI : 10.1016/j.yexcr.2008.05.011

E. Kamynina, K. Kauppinen, F. Duan, N. Muakkassa, and D. Manor, Regulation of Proto-Oncogenic Dbl by Chaperone-Controlled, Ubiquitin-Mediated Degradation, Molecular and Cellular Biology, vol.27, issue.5, pp.1809-1822, 2007.
DOI : 10.1128/MCB.01051-06

D. W. Speicher and V. T. Marchesi, Erythrocyte spectrin is comprised of many homologous triple helical segments, Nature, vol.965, issue.5982, pp.177-180, 1984.
DOI : 10.1038/311177a0

M. D. Baron, M. D. Davison, P. Jones, and D. R. Critchley, The sequence of chick a-actinin reveals homologies to spectrin and calmodulin, J. Biol. Chem, vol.262, pp.17623-17629, 1987.

M. Koenig, A. P. Monaco, and L. M. Kunkel, The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein, Cell, vol.53, issue.2, pp.219-226, 1988.
DOI : 10.1016/0092-8674(88)90383-2

M. D. Davison and D. R. Critchley, ??-actinins and the DMD protein contain spectrin-like repeats, Cell, vol.52, issue.2, pp.159-160, 1988.
DOI : 10.1016/0092-8674(88)90503-X

R. Dubreuil, Structure and evolution of the actin crosslinking proteins, BioEssays, vol.12, issue.5, pp.219-226, 1992.
DOI : 10.1002/bies.950130504

J. Pascual, J. Castresana, and M. Saraste, Evolution of the spectrin repeat, BioEssays, vol.22, issue.9, pp.811-817, 1997.
DOI : 10.1002/bies.950190911

G. Thomas, E. Newbern, C. Korte, M. Bales, S. Muse et al., Intragenic duplication and divergence in the spectrin superfamily of proteins, Molecular Biology and Evolution, vol.14, issue.12, pp.1285-1295, 1997.
DOI : 10.1093/oxfordjournals.molbev.a025738

S. J. Winder, T. J. Gibson, K. , and J. , Dystrophin and utrophin: the missing links! FEBS Lett, pp.27-33, 1995.

S. J. Winder, T. J. Gibson, K. , and J. , Low probability of dystrophin and utrophin coiled coil regions forming dimers, Biochemical Society Transactions, vol.24, issue.2, p.280, 1996.
DOI : 10.1042/bst024280s

S. J. Winder, A. E. Knight, K. , and J. , Protein Structure in: Dystrophin: gene, protein and cell biology, pp.27-55, 1997.

D. A. Parry, T. W. Dixon, and C. Cohen, Analysis of the three-alpha-helix motif in the spectrin superfamily of proteins, Biophysical Journal, vol.61, issue.4, pp.858-867, 1992.
DOI : 10.1016/S0006-3495(92)81893-3

J. Pascual, M. Pfuhl, G. Rivas, A. Pastore, and M. Saraste, The spectrin repeat folds into a three-helix bundle in solution, FEBS Letters, vol.22, issue.3, pp.201-207, 1996.
DOI : 10.1016/0014-5793(96)00251-7

Y. Yan, E. Winograd, A. Viel, T. Cronin, S. C. Harrison et al., Crystal structure of the repetitive segments of spectrin, Science, vol.262, issue.5142, pp.2027-2030, 1993.
DOI : 10.1126/science.8266097

K. Djinovic-carugo, P. Young, M. Gautel, and M. Saraste, Molecular Basis for Cross-Linking of Actin Filaments: Structure of the ??-Actinin Rod, Cell, vol.98, issue.4, pp.537-546, 1999.
DOI : 10.1016/S0092-8674(00)81981-9

V. Grum, D. Li, R. Macdonald, and A. Mondragon, Structures of Two Repeats of Spectrin Suggest Models of Flexibility, Cell, vol.98, issue.4, pp.523-535, 1999.
DOI : 10.1016/S0092-8674(00)81980-7

J. Ylanne, K. Scheffzek, P. Young, and M. Saraste, Crystal Structure of the ??-Actinin Rod Reveals an Extensive Torsional Twist, Structure, vol.9, issue.7, pp.597-604, 2001.
DOI : 10.1016/S0969-2126(01)00619-0

E. Kahana, G. Flood, and W. B. Gratzer, Physical properties of dystrophin rod domain, Cell Motility and the Cytoskeleton, vol.262, issue.3, pp.246-252, 1997.
DOI : 10.1002/(SICI)1097-0169(1997)36:3<246::AID-CM5>3.0.CO;2-5

E. Kahana and W. B. Gratzer, Minimum folding unit of dystrophin rod domain, Biochemistry, vol.34, issue.25, pp.8110-8114, 1995.
DOI : 10.1021/bi00025a017

E. Kahana, P. J. Marsh, A. J. Henry, M. Way, and W. B. Gratzer, Conformation and Phasing of Dystrophin Structural Repeats, Journal of Molecular Biology, vol.235, issue.4, pp.1271-1277, 1994.
DOI : 10.1006/jmbi.1994.1080

R. Calvert, E. Kahana, and W. B. Gratzer, Stability of the dystrophin rod domain fold: evidence for nested repeating units, Biophysical Journal, vol.71, issue.3, pp.1605-1610, 1996.
DOI : 10.1016/S0006-3495(96)79363-3

L. Saadat, L. Pittman, and N. Menhart, Structural cooperativity in spectrin type repeats motifs of dystrophin, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.1764, issue.5, pp.943-954, 2006.
DOI : 10.1016/j.bbapap.2006.02.012

A. Mirza, M. Sagathevan, N. Sahni, L. Choi, and N. Menhart, A biophysical map of the dystrophin rod, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.1804, issue.9, pp.1796-1809, 2010.
DOI : 10.1016/j.bbapap.2010.03.009

L. Rumeur, E. Winder, S. J. Hubert, and J. , Dystrophin: More than just the sum of its parts, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.1804, issue.9, pp.1713-1722, 2010.
DOI : 10.1016/j.bbapap.2010.05.001
URL : https://hal.archives-ouvertes.fr/hal-00592430

B. Legrand, E. Giudice, A. Nicolas, O. Delalande, L. Rumeur et al., Computational Study of the Human Dystrophin Repeats: Interaction Properties and Molecular Dynamics, PLoS ONE, vol.40, issue.8, 2011.
DOI : 10.1371/journal.pone.0023819.s010
URL : https://hal.archives-ouvertes.fr/inserm-00689190

M. Gimona, K. Djinovic-carugo, W. Kranewitter, and S. Winder, Functional plasticity of CH domains, FEBS Letters, vol.50, issue.1, pp.98-106, 2002.
DOI : 10.1016/S0014-5793(01)03240-9

K. J. Amann, B. A. Renley, and J. M. Ervasti, A Cluster of Basic Repeats in the Dystrophin Rod Domain Binds F-actin through an Electrostatic Interaction, Journal of Biological Chemistry, vol.273, issue.43, pp.28419-28423, 1998.
DOI : 10.1074/jbc.273.43.28419

I. N. Rybakova, K. J. Amann, and J. M. Ervasti, A new model for the interaction of dystrophin with F-actin, The Journal of Cell Biology, vol.135, issue.3, pp.661-672, 1996.
DOI : 10.1083/jcb.135.3.661

I. N. Rybakova, J. L. Humston, K. J. Sonnemann, and J. M. Ervasti, Dystrophin and Utrophin Bind Actin through Distinct Modes of Contact, Journal of Biological Chemistry, vol.281, issue.15, pp.9996-10001, 2006.
DOI : 10.1074/jbc.M513121200

K. J. Amann, A. W. Guo, and J. M. Ervasti, Utrophin Lacks the Rod Domain Actin Binding Activity of Dystrophin, Journal of Biological Chemistry, vol.274, issue.50, pp.35375-35380, 1999.
DOI : 10.1074/jbc.274.50.35375

I. N. Rybakova and J. M. Ervasti, Identification of Spectrin-like Repeats Required for High Affinity Utrophin-Actin Interaction, Journal of Biological Chemistry, vol.280, issue.24, pp.23018-23023, 2005.
DOI : 10.1074/jbc.M502530200

X. Li and V. Bennett, Identification of the spectrin subunit and domains required for formation of spectrin/adducin/actin complexes, J. Biol. Chem, vol.271, pp.15695-15702, 1996.

E. Prochniewicz, D. Henderson, J. M. Ervasti, and D. D. Thomas, Dystrophin and utrophin have distinct effects on the structural dynamics of actin, Proc. Nat. Acad. Sci. U S A 106, pp.7822-7827, 2009.
DOI : 10.1073/pnas.0812007106

S. Legardinier, Sub-domains of the dystrophin rod domain display contrasting lipid-binding and stability properties, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.1784, issue.4, pp.672-682, 2008.
DOI : 10.1016/j.bbapap.2007.12.014
URL : https://hal.archives-ouvertes.fr/hal-00457831

S. Legardinier, C. Raguenes-nicol, C. Tascon, C. Rocher, S. Hardy et al., Mapping of the Lipid-Binding and Stability Properties of the Central Rod Domain of Human Dystrophin, Journal of Molecular Biology, vol.389, issue.3, pp.546-558, 2009.
DOI : 10.1016/j.jmb.2009.04.025
URL : https://hal.archives-ouvertes.fr/inserm-00404317

V. Vie, Specific anchoring modes of two distinct dystrophin rod sub-domains interacting in phospholipid Langmuir films studied by atomic force microscopy and PM-IRRAS, Biochimica et Biophysica Acta (BBA) - Biomembranes, vol.1798, issue.8, pp.1503-1511, 2010.
DOI : 10.1016/j.bbamem.2010.04.005
URL : https://hal.archives-ouvertes.fr/hal-00492227

A. Czogalla, K. Grzymajlo, A. Jezierski, and A. F. Sikorski, Phospholipid-induced structural changes to an erythroid ?? spectrin ankyrin-dependent lipid-binding site, Biochimica et Biophysica Acta (BBA) - Biomembranes, vol.1778, issue.11, pp.2612-2620, 2008.
DOI : 10.1016/j.bbamem.2008.07.020

J. Sarkis, Spectrin-like Repeats 11-15 of Human Dystrophin Show Adaptations to a Lipidic Environment, Journal of Biological Chemistry, vol.286, issue.35, pp.30481-30491, 2011.
DOI : 10.1074/jbc.M111.243881
URL : https://hal.archives-ouvertes.fr/inserm-00712828

J. Sarkis, V. Vié, S. J. Winder, A. Renault, E. L. Rumeur et al., Resisting sarcolemmal rupture: dystrophin repeats increase membrane-actin stiffness, The FASEB Journal, vol.27, issue.1
DOI : 10.1096/fj.12-208967
URL : https://hal.archives-ouvertes.fr/hal-00806086

J. S. Stamler and G. Meissner, Physiology of nitric oxide in skeletal muscle, Physiol. Rev, vol.81, pp.209-237, 2001.

J. A. Brenman, D. S. Chao, H. Xia, K. Aldape, and D. S. Bredt, Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy, Cell, vol.82, issue.5, pp.743-752, 1995.
DOI : 10.1016/0092-8674(95)90471-9

S. Torelli, S. C. Brown, C. Jimenez-mallebrera, L. Feng, F. Muntoni et al., Absence of neuronal nitric oxide synthase (nNOS) as a pathological marker for the diagnosis of Becker muscular dystrophy with rod domain deletions, Neuropathology and Applied Neurobiology, vol.2, issue.5, pp.540-545, 2004.
DOI : 10.1096/fj.02-0519com

D. Chao, Selective loss of sarcolemmal nitric oxide synthase in Becker muscular dystrophy, Journal of Experimental Medicine, vol.184, issue.2, pp.609-618, 1996.
DOI : 10.1084/jem.184.2.609

M. E. Adams, H. A. Mueller, and S. C. Froehner, In vivo requirement of the ??-syntrophin PDZ domain for the sarcolemmal localization of nNOS and aquaporin-4, The Journal of Cell Biology, vol.76, issue.1, pp.113-122, 2001.
DOI : 10.1083/jcb.200106158

Y. Lai, Dystrophins carrying spectrin-like repeats 16 and 17 anchor nNOS to the sarcolemma and enhance exercise performance in a mouse model of muscular dystrophy, Journal of Clinical Investigation, vol.119, issue.3, pp.624-635, 2009.
DOI : 10.1172/JCI36612DS1

A. Goyenvalle, J. T. Seto, K. E. Davies, and J. Chamberlain, Therapeutic approaches to muscular dystrophy, Human Molecular Genetics, vol.20, issue.R1, pp.69-78, 2011.
DOI : 10.1093/hmg/ddr105
URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3095062

T. Pawson and P. Nash, Assembly of Cell Regulatory Systems Through Protein Interaction Domains, Science, vol.300, issue.5618, pp.445-452, 2003.
DOI : 10.1126/science.1083653

B. Sha, S. E. Phillips, V. A. Bankaitis, and M. Luo, Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein, Nature, vol.391, pp.506-510, 1998.

C. P. Ponting, D. J. Blake, K. E. Davies, J. Kendrick-jones, and S. J. Winder, ZZ and TAZ: new putative zinc fingers in dystrophin and other proteins, Trends in Biochemical Sciences, vol.21, issue.1, pp.11-13, 1996.
DOI : 10.1016/S0968-0004(06)80020-4

J. Sodek, R. S. Hodges, L. B. Smillie, and L. Jurasek, Amino-Acid Sequence of Rabbit Skeletal Tropomyosin and Its Coiled-Coil Structure, Proceedings of the National Academy of Sciences, vol.69, issue.12, pp.3800-3804, 1972.
DOI : 10.1073/pnas.69.12.3800

J. Castresana and M. Saraste, Does Vav bind to F-actin through a CH domain?, FEBS Letters, vol.256, issue.2, pp.149-151, 1995.
DOI : 10.1016/0014-5793(95)01098-Y

D. Ron, A region of proto-dbl essential for its transforming activity shows sequence similarity to a yeast cell cycle gene, CDC24, and the human breakpoint cluster gene, bcr, New Biol, vol.3, pp.372-379, 1991.

R. M. Tufty and R. H. Kretsinger, Troponin and parvalbumin calcium binding regions predicted in myosin light chain and T4 lysozyme, Science, vol.187, issue.4172, pp.167-169, 1975.
DOI : 10.1126/science.1111094

B. J. Mayer, R. Ren, K. L. Clark, and D. Baltimore, A putative modular domain present in diverse signaling proteins, Cell, vol.73, issue.4, pp.629-630, 1993.
DOI : 10.1016/0092-8674(93)90244-K

R. J. Haslam, H. B. Koide, and B. A. Hemmings, Pleckstrin domain homology, Nature, vol.363, issue.6427, pp.309-310, 1993.
DOI : 10.1038/363309b0

G. Wiche, B. Becker, K. Luber, G. Weitzer, M. J. Castanon et al., Cloning and sequencing of rat plectin indicates a 466-kD polypeptide chain with a three-domain structure based on a central alpha-helical coiled coil, The Journal of Cell Biology, vol.114, issue.1, pp.83-99, 1991.
DOI : 10.1083/jcb.114.1.83

M. L. Stahl, C. R. Ferenz, K. L. Kelleher, R. W. Kriz, and J. L. Knopf, Sequence similarity of phospholipase C with the non-catalytic region of src, Nature, vol.332, issue.6161, pp.269-272, 1988.
DOI : 10.1038/332269a0

B. J. Mayer, M. Hamaguchi, and H. Hanafusa, A novel viral oncogene with structural similarity to phospholipase C, Nature, vol.332, issue.6161, pp.272-275, 1988.
DOI : 10.1038/332272a0

P. Bork and M. Sudol, The WW domain: a signalling site in dystrophin?, Trends in Biochemical Sciences, vol.19, issue.12, pp.531-533, 1994.
DOI : 10.1016/0968-0004(94)90053-1

H. Kusunoki, G. Minasov, R. I. Macdonald, and A. Mondragon, Independent Movement, Dimerization and Stability of Tandem Repeats of Chicken Brain ??-Spectrin, Journal of Molecular Biology, vol.344, issue.2, pp.495-511, 2004.
DOI : 10.1016/j.jmb.2004.09.019

M. Koenig and L. M. Kunkel, Detailed analysis of the repeat domain of dystrophin reveals four potential hinge segments that may confer flexibility, J. Biol. Chem, vol.265, pp.4560-4566, 1990.

N. Menhart, Hybrid spectrin type repeats produced by exon-skipping in dystrophin, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.1764, issue.6, pp.993-999, 2006.
DOI : 10.1016/j.bbapap.2006.03.017

M. Way, B. Pope, R. A. Cross, J. Kendrick-jones, and A. G. Weeds, and demonstration of binding to F-actin, FEBS Letters, vol.349, issue.3, pp.243-245, 1992.
DOI : 10.1016/0014-5793(92)80249-G

S. Rentschler, H. Linn, K. Deininger, M. T. Bedford, X. Espanel et al., The WW domain of dystrophin requires EF-hands region to interact with beta-dystroglycan, Biol. Chem, vol.380, pp.431-442, 1999.