Intermediate filament-like protein syncoilin in normal and myopathic striated muscle

Neuromuscular Disorders

Volumn 17, Issue 11-12, 2007, Pages 970-979

  McCullagh, Karl J A ^a   Edwards, Ben ^a   Poon, Ellen ^a   Lovering, Richard M ^a   Paulin, Denise ^b   Davies, Kay E ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITÉ PARIS DESCARTES   (France)

Author keywords

Dystrophy; Muscle fiber type; Myopathy; Myotendinous junction; Z lines

Indexed keywords

ALPHA DYSTROBREVIN; DESMIN; DYSTROBREVIN; INTERMEDIATE FILAMENT PROTEIN; SYNCOILIN; UNCLASSIFIED DRUG;

ANIMAL TISSUE; ARTICLE; CELLULAR DISTRIBUTION; CONTROLLED STUDY; CYTOPLASM; CYTOSKELETON; MOUSE; MUSCLE CELL; MUSCULAR DYSTROPHY; MYOPATHY; NEUROMUSCULAR SYNAPSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; SARCOLEMMA; SARCOPLASM; SKELETAL MUSCLE;

ANIMALS; CYTOPLASM; DESMIN; DYSTROPHIN-ASSOCIATED PROTEINS; INTERMEDIATE FILAMENT PROTEINS; MICE; MICE, INBRED C57BL; MICE, KNOCKOUT; MICROSCOPY, ELECTRON, TRANSMISSION; MUSCLE FIBERS; MUSCLE PROTEINS; MUSCLE, STRIATED; MUSCULAR DISEASES; NEUROMUSCULAR JUNCTION; SARCOLEMMA; SARCOMERES; UP-REGULATION;

EID: 36249026292     PISSN: 09608966     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.nmd.2007.06.004     Document Type: Article

References (37)

1. Dalkilic I., and Kunkel L.M. Muscular dystrophies: genes to pathogenesis. Curr Opin Genet Dev 13 (2003) 231-238
2. Rando T.A. The dystrophin-glycoprotein complex, cellular signaling, and the regulation of cell survival in the muscular dystrophies. Muscle Nerve 24 (2001) 1575-1594
3. Grady R.M., Grange R.W., Lau K.S., et al. Role for alpha-dystrobrevin in the pathogenesis of dystrophin-dependent muscular dystrophies. Nat Cell Biol 1 (1999) 215-220
4. Grady R.M., Zhou H., Cunningham J.M., Henry M.D., Campbell K.P., and Sanes J.R. Maturation and maintenance of the neuromuscular synapse: genetic evidence for roles of the dystrophin-glycoprotein complex. Neuron 25 (2000) 279-293
5. Blake D.J., and Martin-Rendon E. Intermediate filaments and the function of the dystrophin-protein complex. Trends Cardiovasc Med 12 (2002) 224-228
6. Albrecht D.E., and Froehner S.C. DAMAGE, a novel alpha-dystrobrevin-associated MAGE protein in dystrophin complexes. J Biol Chem 279 (2004) 7014-7023
7. Omary M.B., Coulombe P.A., and McLean W.H. Intermediate filament proteins and their associated diseases. N Engl J Med 351 (2004) 2087-2100
8. Newey S.E., Howman E.V., Ponting C.P., et al. Syncoilin, a novel member of the intermediate filament superfamily that interacts with alpha-dystrobrevin in skeletal muscle. J Biol Chem 276 (2001) 6645-6655
9. Poon E., Howman E.V., Newey S.E., and Davies K.E. Association of syncoilin and desmin: linking intermediate filament proteins to the dystrophin-associated protein complex. J Biol Chem 277 (2002) 3433-3439
10. Mermelstein C.S., Andrade L.R., Portilho D.M., and Costa M.L. Desmin filaments are stably associated with the outer nuclear surface in chick myoblasts. Cell Tissue Res (2005) 1-7
11. Tolstonog G.V., Sabasch M., and Traub P. Cytoplasmic intermediate filaments are stably associated with nuclear matrices and potentially modulate their DNA-binding function. DNA Cell Biol 21 (2002) 213-239
12. Li Z., Mericskay M., Agbulut O., et al. Desmin is essential for the tensile strength and integrity of myofibrils but not for myogenic commitment, differentiation, and fusion of skeletal muscle. J Cell Biol 139 (1997) 129-144
13. Milner D.J., Weitzer G., Tran D., Bradley A., and Capetanaki Y. Disruption of muscle architecture and myocardial degeneration in mice lacking desmin. J Cell Biol 134 (1996) 1255-1270
14. Blake D.J., Nawrotzki R., Loh N.Y., Gorecki D.C., and Davies K.E. Beta-dystrobrevin, a member of the dystrophin-related protein family. Proc Natl Acad Sci USA 95 (1998) 241-246
15. Schiaffino S., Gorza L., Sartore S., et al. Three myosin heavy chain isoforms in type 2 skeletal muscle fibres. J Muscle Res Cell Motil 10 (1989) 197-205
16. Brown L.D., and Schneider M.F. Delayed dedifferentiation and retention of properties in dissociated adult skeletal muscle fibers in vitro. In Vitro Cell Dev Biol Anim 38 (2002) 411-422
17. Woods C.E., Novo D., DiFranco M., and Vergara J.L. The action potential-evoked sarcoplasmic reticulum calcium release is impaired in mdx mouse muscle fibres. J Physiol 557 (2004) 59-75
18. Cheng T.J., Lin Y.L., Chiang A.S., and Lai Y.K. Association of protein phosphatase 2A with its substrate vimentin intermediate filaments in 9L rat brain tumor cells. J Cell Biochem 79 (2000) 126-138
19. Allen D.L., Harrison B.C., Sartorius C., Byrnes W.C., and Leinwand L.A. Mutation of the IIB myosin heavy chain gene results in muscle fiber loss and compensatory hypertrophy. Am J Physiol Cell Physiol 280 (2001) C637-C645
20. Burkholder T.J., Fingado B., Baron S., and Lieber R.L. Relationship between muscle fiber types and sizes and muscle architectural properties in the mouse hindlimb. J Morphol 221 (1994) 177-190
21. Lieber R.L., and Friden J. Functional and clinical significance of skeletal muscle architecture. Muscle Nerve 23 (2000) 1647-1666
22. Grady R.M., Akaaboune M., Cohen A.L., Maimone M.M., Lichtman J.W., and Sanes J.R. Tyrosine-phosphorylated and nonphosphorylated isoforms of alpha-dystrobrevin: roles in skeletal muscle and its neuromuscular and myotendinous junctions. J Cell Biol 160 (2003) 741-752
23. Chopard A., Pons F., and Marini J.F. Cytoskeletal protein contents before and after hindlimb suspension in a fast and slow rat skeletal muscle. Am J Physiol Regul Integr Comp Physiol 280 (2001) R323-R330
24. Iwaki T., Iwaki A., and Goldman J.E. Alpha B-crystallin in oxidative muscle fibers and its accumulation in ragged-red fibers: a comparative immunohistochemical and histochemical study in human skeletal muscle. Acta Neuropathol (Berl) 85 (1993) 475-480
25. Balogh J., Li Z., Paulin D., and Arner A. Lower active force generation and improved fatigue resistance in skeletal muscle from desmin deficient mice. J Muscle Res Cell Motil 24 (2003) 453-459
26. Wu H., Naya F.J., McKinsey T.A., et al. MEF2 responds to multiple calcium-regulated signals in the control of skeletal muscle fiber type. EMBO J 19 (2000) 1963-1973
27. Kuisk I.R., Li H., Tran D., and Capetanaki Y. A single MEF2 site governs desmin transcription in both heart and skeletal muscle during mouse embryogenesis. Dev Biol 174 (1996) 1-13
28. Milner D.J., Mavroidis M., Weisleder N., and Capetanaki Y. Desmin cytoskeleton linked to muscle mitochondrial distribution and respiratory function. J Cell Biol 150 (2000) 1283-1298
29. Carlsson L., Li Z.L., Paulin D., et al. Differences in the distribution of synemin, paranemin, and plectin in skeletal muscles of wild-type and desmin knock-out mice. Histochem Cell Biol 114 (2000) 39-47
30. Mizuno Y., Guyon J.R., Watkins S.C., et al. Beta-synemin localizes to regions of high stress in human skeletal myofibers. Muscle Nerve 30 (2004) 337-346
31. Deconinck A.E., Rafael J.A., Skinner J.A., et al. Utrophin-dystrophin-deficient mice as a model for Duchenne muscular dystrophy. Cell 90 (1997) 717-727
32. Ralston E., Lu Z., Biscocho N., et al. Blood vessels and desmin control the positioning of nuclei in skeletal muscle fibers. J Cell Physiol (2006)
33. Shah S.B., Davis J., Weisleder N., et al. Structural and functional roles of desmin in mouse skeletal muscle during passive deformation. Biophys J 86 (2004) 2993-3008
34. Wilding J.R., Schneider J.E., Sang A.E., Davies K.E., Neubauer S., and Clarke K. Dystrophin- and MLP-deficient mouse hearts: marked differences in morphology and function, but similar accumulation of cytoskeletal proteins. FASEB J 19 (2005) 79-81
35. Mizuno Y., Thompson T.G., Guyon J.R., et al. Desmuslin, an intermediate filament protein that interacts with alpha -dystrobrevin and desmin. Proc Natl Acad Sci USA 98 (2001) 6156-6161
36. Elder G.A., Friedrich Jr. V.L., Bosco P., et al. Absence of the mid-sized neurofilament subunit decreases axonal calibers, levels of light neurofilament (NF-L), and neurofilament content. J Cell Biol 141 (1998) 727-739
37. Reichelt J., Bussow H., Grund C., and Magin T.M. Formation of a normal epidermis supported by increased stability of keratins 5 and 14 in keratin 10 null mice. Mol Biol Cell 12 (2001) 1557-1568