Muscle intermediate filaments and their links to membranes and membranous organelles

Experimental Cell Research

Volumn 313, Issue 10, 2007, Pages 2063-2076

  Capetanaki, Yassemi ^a   Bloch, Robert J ^b   Kouloumenta, Asimina ^a   Mavroidis, Manolis ^a   Psarras, Stelios ^a  

^a Academy of Athens Biomedical Research Foundation   (Greece)

^b UNIVERSITY OF MARYLAND SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DESMIN;

CELL DIFFERENTIATION; CELL ENERGY; CELL FUSION; CELL GROWTH; CELL NUCLEUS; CELL ORGANELLE; ENERGY YIELD; GENE EXPRESSION; HUMAN; LYSOSOME; MEMBRANE VESICLE; MITOCHONDRION; MYOBLAST; MYOFILAMENT; NONHUMAN; PRIORITY JOURNAL; REVIEW; SARCOLEMMA;

EID: 34249697100     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2007.03.033     Document Type: Review

References (167)

1. Lazarides E. Intermediate filaments as mechanical integrators of cellular space. Nature 283 (1980) 249-256
2. Georgatos S.D., and Maison C. Integration of intermediate filaments into cellular organelles. Int. Rev. Cytol. 164 (1996) 91-138
3. Granger B.L., and Lazarides E. Synemin: a new high molecular weight protein associated with desmin and vimentin filaments in muscle. Cell 22 (1980) 727-738
4. Capetanaki Y., and Milner D.J. Desmin cytoskeleton in muscle integrity and function. Subcell Biochem. 31 (1998) 463-495
5. Fuchs E., and Clevel D.W. A structural scaffolding of intermediate filaments in health and disease. Science 279 (1998) 514-519
6. Capetanaki Y. Desmin cytoskeleton: a potential regulator of muscle mitochondrial behavior and function. Trends Cardiovasc. Med. 12 (2002) 339-348
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. Paulin D., Huet A., Khanamyrian L., and Xue Z. Desminopathies in muscle disease. J. Pathol. 204 (2004) 418-427
9. Toivola D.M., Tao G.Z., Habtezion A., Liao J., and Omary M.B. Cellular integrity plus: organelle-related and protein-targeting functions of intermediate filaments. Trends Cell Biol. 15 (2005) 608-617
10. Lazarides E. Intermediate filaments: a chemically heterogeneous, developmentally regulated class of proteins. Annu. Rev. Biochem. 51 (1982) 219-250
11. Bilak S.R., Sernett S.W., Bilak M.M., Bellin R.M., Stromer M.H., Huiatt T.W., and Robson R.M. Properties of the novel intermediate filament protein synemin and its identification in mammalian muscle. Arch. Biochem. Biophys. 355 (1998) 63-76
12. Mizuno Y., Thompson T.G., Guyon J.R., Lidov H.G., Brosius M., Imamura M., Ozawa E., Watkins S.C., and Kunkel L.M. Desmuslin, an intermediate filament protein that interacts with alpha-dystrobrevin and desmin. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 6156-6161
13. Titeux M., Brocheriou V., Xue Z., Gao J., Pellissier J.F., Guicheney P., Paulin D., and Li Z. Human synemin gene generates splice variants encoding two distinct intermediate filament proteins. Eur. J. Biochem. 268 (2001) 6435-6449
14. Price M.G., and Lazarides E. Expression of intermediate filament-associated proteins paranemin and synemin in chicken development. J. Cell Biol. 97 (1983) 1860-1874
15. Schweitzer S.C., Klymkowsky M.W., Bellin R.M., Robson R.M., Capetanaki Y., and Evans R.M. Paranemin and the organization of desmin filament networks. J. Cell Sci. 114 (2001) 1079-1089
16. Bellin R.M., Huiatt T.W., Critchley D.R., and Robson R.M. Synemin may function to directly link muscle cell intermediate filaments to both myofibrillar Z-lines and costameres. J. Biol. Chem. 276 (2001) 32330-32337
17. Newey S.E., Howman E.V., Ponting C.P., Benson M.A., Nawrotzki R., Loh N.Y., Davies K.E., and Blake D.J. Syncoilin, a novel member of the intermediate filament superfamily that interacts with alpha-dystrobrevin in skeletal muscle. J. Biol. Chem. 276 (2001) 6645-6655
18. Carlsson L., Li Z.L., Paulin D., Price M.G., Breckler J., Robson R.M., Wiche G., and Thornell L.E. 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
19. Sejersen T., and Lendahl U. Transient expression of the intermediate filament nestin during skeletal muscle development. J. Cell Sci. 106 Pt 4 (1993) 1291-1300
20. Kachinsky A.M., Dominov J.A., and Miller J.B. Myogenesis and the intermediate filament protein, nestin. Dev. Biol. 165 (1994) 216-228
21. Steinert P.M., Marekov L.N., and Parry D.A. Molecular parameters of type IV alpha-internexin and type IV-type III alpha-internexin-vimentin copolymer intermediate filaments. J. Biol. Chem. 274 (1999) 1657-1666
22. Vaittinen S., Lukka R., Sahlgren C., Hurme T., Rantanen J., Lendahl U., Eriksson J.E., and Kalimo H. The expression of intermediate filament protein nestin as related to vimentin and desmin in regenerating skeletal muscle. J. Neuropathol. Exp. Neurol. 60 (2001) 588-597
23. Carlsson L., Li Z., Paulin D., and Thornell L.E. Nestin is expressed during development and in myotendinous and neuromuscular junctions in wild type and desmin knock-out mice. Exp. Cell Res. 251 (1999) 213-223
24. Fuchs E., and Weber K. Intermediate filaments: structure, dynamics, function, and disease. Annu. Rev. Biochem. 63 (1994) 345-382
25. Capetanaki Y., Starnes S., and Smith S. Expression of the chicken vimentin gene in transgenic mice: efficient assembly of the avian protein into the cytoskeleton. Proc. Natl. Acad. Sci. U. S. A. 86 (1989) 4882-4886
26. 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
27. Xue Z.G., Cheraud Y., Brocheriou V., Izmiryan A., Titeux M., Paulin D., and Li Z. The mouse synemin gene encodes three intermediate filament proteins generated by alternative exon usage and different open reading frames. Exp. Cell Res. 298 (2004) 431-444
28. Ursitti J.A., Lee P.C., Resneck W.G., McNally M.M., Bowman A.L., O'Neill A., Stone M.R., and Bloch R.J. Cloning and characterization of cytokeratins 8 and 19 in adult rat striated muscle. Interaction with the dystrophin glycoprotein complex. J. Biol. Chem. 279 (2004) 41830-41838
29. Kaufman S.J., and Foster R.F. Replicating myoblasts express a muscle-specific phenotype. Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 9606-9610
30. Herrmann H., Fouquet B., and Franke W.W. Expression of intermediate filament proteins during development of Xenopus laevis. I. CDNA clones encoding different forms of vimentin. Development 105 (1989) 279-298
31. 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
32. Allen R.E., Rankin L.L., Greene E.A., Boxhorn L.K., Johnson S.E., Taylor R.G., and Pierce P.R. Desmin is present in proliferating rat muscle satellite cells but not in bovine muscle satellite cells. J. Cell Physiol. 149 (1991) 525-535
33. Olson E.N. Myod family: a paradigm for development?. Genes Dev. 4 (1990) 1454-1461
34. Lyon G.E., and Buckingham M.E. Myogenic factor gene expression in mouse somites and limb buds. Mol. Basis Morphogen (1993) 155-164
35. Li H., and Capetanaki Y. Regulation of the mouse desmin gene: transactivated by Myod, myogenin, Mrf4 and Myf5. Nucleic Acids Res. 21 (1993) 335-343
36. Perriard J.C., Hirschy A., and Ehler E. Dilated cardiomyopathy: a disease of the intercalated disc?. Trends Cardiovasc. Med. 13 (2003) 30-38
37. Franke W.W., Borrmannn C.M., Grund C., and Pieperhoff S. The area composita of adhering junctions connecting heart muscle cells of vertebrate. I. Molecular definition in intercalated discs of cardiomyocytes by immunoelectron microscopy of desmosomal proteins. Eur. J. Cell Biol. 85 (2006) 69-82
38. Saetersdal T., Dalen H., and Roli J. Immunofluorescence and immunogold electron microscopy of desmin in isolated adult heart myocytes of the rat. Histochemistry 92 (1989) 467-473
39. Mizuno Y., Guyon J.R., Watkins S.C., Mizushima K., Sasaoka T., Imamura M., Kunkel L.M., and Okamoto K. Beta-synemin localizes to regions of high stress in human skeletal myofibers. Muscle Nerve 30 (2004) 337-346
40. Lazarides E., and Hubbard B.D. Immunological characterization of the subunit of the 100 a filaments from muscle cells. Proc. Natl. Acad. Sci. U. S. A. 73 (1976) 4344-4348
41. O'Neill A., Williams M.W., Resneck W.G., Milner D.J., Capetanaki Y., and Bloch R.J. Sarcolemmal organization in skeletal muscle lacking desmin: evidence for cytokeratins associated with the membrane skeleton at costameres. Mol. Biol. Cell 13 (2002) 2347-2359
42. Sam M., Shah S., Friden J., Milner D.J., Capetanaki Y., and Lieber R.L. Desmin knockout muscles generate lower stress and are less vulnerable to injury compared with wild-type muscles. Am. J. Physiol.: Cell Physiol. 279 (2000) C1116-C1122
43. Bhosle R.C., Michele D.E., Campbell K.P., Li Z., and Robson R.M. Interactions of intermediate filament protein synemin with dystrophin and utrophin. Biochem. Biophys. Res. Commun. 346 (2006) 768-777
44. Stone M.R., O'Neill A., Catino D., and Bloch R.J. Specific interaction of the actin-binding domain of dystrophin with intermediate filaments containing keratin 19. Mol. Biol. Cell 16 (2005) 4280-4293
45. Steinbock F.A., and Wiche G. Plectin: a cytolinker by design. Biol. Chem. 380 (1999) 151-158
46. Hijikata T., Murakami T., Ishikawa H., and Yorifuji H. Plectin tethers desmin intermediate filaments onto subsarcolemmal dense plaques containing dystrophin and vinculin. Histochem. Cell Biol. 119 (2003) 109-123
47. Vajsar J., Becker L.E., Freedom R.M., and Murphy E.G. Familial desminopathy: myopathy with accumulation of desmin-type intermediate filaments. J. Neurol., Neurosurg. Psychiatry 56 (1993) 644-648
48. McMillan J.R., Akiyama M., Rouan F., Mellerio J.E., Lane E.B., Leigh I.M., Owaribe K., Wiche G., Fujii N., Uitto J., Eady R.A., and Shimizu H. Plectin defects in epidermolysis bullosa simplex with muscular dystrophy. Muscle Nerve 35 (2007) 24-35
49. Li H., Choudhary S.K., Milner D.J., Munir M.I., Kuisk I.R., and Capetanaki Y. Inhibition of desmin expression blocks myoblast fusion and interferes with the myogenic regulators Myod and Myogenin. J. Cell Biol. 124 (1994) 827-841
50. Weitzer G., Milner D.J., Kim J.U., Bradley A., and Capetanaki Y. Cytoskeletal control of myogenesis: a desmin null mutation blocks the myogenic pathway during embryonic stem cell differentiation. Dev. Biol. 172 (1995) 422-439
51. Capetanaki Y. Desmin cytoskeleton in healthy and failing heart. Heart Fail. Rev. 5 (2000) 203-220
52. Wakelam M.J. The fusion of myoblasts. Biochem. J. 228 (1985) 1-12
53. Krimpenfort P.J., Schaart G., Pieper F.R., Ramaekers F.C., Cuypers H.T., van den Heuvel R.M., Vree Egberts W.T., van Eys G.J., Berns A., and Bloemendal H. Tissue-specific expression of a vimentin-desmin hybrid gene in transgenic mice. EMBO J. 7 (1988) 941-947
54. Choi J., Costa M.L., Mermelstein C.S., Chagas C., Holtzer S., and Holtzer H. Myod converts primary dermal fibroblasts, chondroblasts, smooth muscle, and retinal pigmented epithelial cells into striated mononucleated myoblasts and multinucleated myotubes. Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 7988-7992
55. Tao J.X., and Ip W. Site-specific antibodies block kinase a phosphorylation of desmin in vitro and inhibit incorporation of myoblasts into myotubes. Cell Motil. Cytoskeleton 19 (1991) 109-120
56. Camargo F.D., Green R., Capetanaki Y., Jackson K.A., and Goodell M.A. Single hematopoietic stem cells generate skeletal muscle through myeloid intermediates. Nat. Med. 9 (2003) 1520-1527
57. Chen E.H., and Olson E.N. Unveiling the mechanisms of cell-cell fusion. Science 308 (2005) 369-373
58. 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. 323 (2006) 351-357
59. Franke W.W. Relationship of nuclear membranes with filaments and microtubules. Protoplasma 73 (1971) 263-292
60. Crisp M., Liu Q., Roux K., Rattner J.B., Shanahan C., Burke B., Stahl P.D., and Hodzic D. Coupling of the nucleus and cytoplasm: role of the Linc complex. J. Cell Biol. 172 (2006) 41-53
61. Tzur Y.B., Wilson K.L., and Gruenbaum Y. Sun-domain proteins: 'Velcro' that links the nucleoskeleton to the cytoskeleton. Nat. Rev., Mol. Cell Biol. 7 (2006) 782-788
62. 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
63. Lockard V.G., and Bloom S. Trans-cellular desmin-lamin B intermediate filament network in cardiac myocytes. J. Mol. Cell Cardiol. 25 (1993) 303-309
64. Georgatos S.D., Weber K., Geisler N., and Blobel G. Binding of two desmin derivatives to the plasma membrane and the nuclear envelope of avian erythrocytes: evidence for a conserved site-specificity in intermediate filament-membrane interactions. Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 6780-6784
65. Capetanaki Y., Milner D.J., and Weitzer G. Desmin in muscle formation and maintenance: knockouts and consequences. Cell Structure and Function 22 (1997) 103-116
66. Shah S.B., Davis J., Weisleder N., Kostavassili I., McCulloch A.D., Ralston E., Capetanaki Y., and Lieber R.L. Structural and functional roles of desmin in mouse skeletal muscle during passive deformation. Biophys. J. 86 (2004) 2993-3008
67. Ralston E., Lu Z., Biscocho N., Soumaka E., Mavroidis M., Prats C., Lomo T., Capetanaki Y., and Ploug T. Blood vessels and desmin control the positioning of nuclei in skeletal muscle fibers. J. Cell Physiol. 209 (2006) 874-882
68. Nikolova V., Leimena C., McMahon A.C., Tan J.C., Chandar S., Jogia D., Kesteven S.H., Michalicek J., Otway R., Verheyen F., Rainer S., Stewart C.L., Martin D., Feneley M.P., and Fatkin D. Defects in nuclear structure and function promote dilated cardiomyopathy in lamin A/C-deficient mice. J. Clin. Invest. 113 (2004) 357-369
69. Frock R.L., Kudlow B.A., Evans A.M., Jameson S.A., Hauschka S.D., and Kennedy B.K. Lamin A/C and emerin are critical for skeletal muscle satellite cell differentiation. Genes Dev. 20 (2006) 486-500
70. A. Hollrigl, M. Hofner, M. Hofner, G. Weitzer, Differentiation of cardiomyocytes requires functional serine residues within the amino-terminal domain of desmin, Differentiation Mar 23; PMID 17381546.
71. M. Hofner, A. Hollrigl, S. Puz, M. Stary, G. Weitzer, Desmin stimulates differentiation of cardiomyocytes and up-regulation of brachyury and Nkx.2.5. Differentiation Mar 23; PMID 17381547.
72. Gerace L., and Burke B. Functional organization of the nuclear envelope. Annu. Rev. Cell Biol. 4 (1988) 335-374
73. Wilhelmsen K., Ketema M., Truong H., and Sonnenberg A. Kash-domain proteins in nuclear migration, anchorage and other processes. J. Cell Sci. 119 (2006) 5021-5029
74. Wilhelmsen K., Litjens S.H., Kuikman I., Tshimbalanga N., Janssen H., van den Bout I., Raymond K., and Sonnenberg A. Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin. J. Cell Biol. 171 (2005) 799-810
75. Houben F., Ramaekers F.C., Snoeckx L.H., and Broers J.L. Role of nuclear lamina-cytoskeleton interactions in the maintenance of cellular strength. Biochim. Biophys. Acta 1773 (2007) 675-686
76. Rappaport L., Oliviero P., and Samuel J.L. Cytoskeleton and mitochondrial morphology and function. Mol. Cell Biochem. 184 (1998) 101-105
77. Anesti V., and Scorrano L. The relationship between mitochondrial shape and function and the cytoskeleton. Biochim. Biophys. Acta 1757 (2006) 692-699
78. 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
79. Milner D.J., Taffet G.E., Wang X., Pham T., Tamura T., Hartley C., Gerdes A.M., and Capetanaki Y. The absence of desmin leads to cardiomyocyte hypertrophy and cardiac dilation with compromised systolic function. J. Mol. Cell. Cardiol. 31 (1999) 2063-2076
80. 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
81. Mavroidis M., and Capetanaki Y. Extensive induction of important mediators of fibrosis and dystrophic calcification in desmin-deficient cardiomyopathy. Am. J. Pathol. 160 (2002) 943-952
82. Kay L., Li Z., Mericskay M., Olivares J., Tranqui L., Fontaine E., Tiivel T., Sikk P., Kaambre T., Samuel J.L., Rappaport L., Usson Y., Leverve X., Paulin D., and Saks V.A. Study of regulation of mitochondrial respiration in vivo. An analysis of influence of Adp diffusion and possible role of cytoskeleton. Biochim. Biophys. Acta 1322 (1997) 41-59
83. Schroder R., Goudeau B., Simon M.C., Fischer D., Eggermann T., Clemen C.S., Li Z., Reimann J., Xue Z., Rudnik-Schoneborn S., Zerres K., van der Ven P.F., Furst D.O., Kunz W.S., and Vicart P. On noxious desmin: functional effects of a novel heterozygous desmin insertion mutation on the extrasarcomeric desmin cytoskeleton and mitochondria. Hum. Mol. Genet. 12 (2003) 657-669
84. Brownlees J., Ackerley S., Grierson A.J., Jacobsen N.J., Shea K., Anderton B.H., Leigh P.N., Shaw C.E., and Miller C.C. Charcot-Marie-Tooth disease neurofilament mutations disrupt neurofilament assembly and axonal transport. Hum. Mol. Genet. 11 (2002) 2837-2844
85. Perez-Olle R., Lopez-Toledano M.A., Goryunov D., Cabrera-Poch N., Stefanis L., Brown K., and Liem R.K. Mutations in the neurofilament light gene linked to Charcot-Marie-Tooth disease cause defects in transport. J. Neurochem. 93 (2005) 861-874
86. Uttam J., Hutton E., Coulombe P.A., Anton-Lamprecht I., Yu Q.C., Gedde-Dahl Jr. T., Fine J.D., and Fuchs E. The genetic basis of epidermolysis bullosa simplex with mottled pigmentation. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 9079-9084
87. Palmer J.W., Tandler B., and Hoppel C.L. Heterogeneous response of subsarcolemmal heart mitochondria to calcium. Am. J. Physiol. 250 (1986) H741-H748
88. Lesnefsky E.J., Moghaddas S., Tandler B., Kerner J., and Hoppel C.L. Mitochondrial dysfunction in cardiac disease: ischemia-reperfusion, aging, and heart failure. J. Mol. Cell Cardiol. 33 (2001) 1065-1089
89. Levine T., and Rabouille C. Endoplasmic reticulum: one continuous network compartmentalized by extrinsic cues. Curr. Opin. Cell Biol. 17 (2005) 362-368
90. Brough D., Sim Y., Thorn P., and Irvine R.F. The structural integrity of the endoplasmic reticulum, and its possible regulation by inositol 1,3,4,5-tetrakisphosphate. Cell Calcium 38 (2005) 153-159
91. Vance J.E. Phospholipid synthesis in a membrane fraction associated with mitochondria. J. Biol. Chem. 265 (1990) 7248-7256
92. Filippin L., Magalhaes P.J., Di Benedetto G., Colella M., and Pozzan T. Stable interactions between mitochondria and endoplasmic reticulum allow rapid accumulation of calcium in a subpopulation of mitochondria. J. Biol. Chem. 278 (2003) 39224-39234
93. Wang H.J., Guay G., Pogan L., Sauve R., and Nabi I.R. Calcium regulates the association between mitochondria and a smooth subdomain of the endoplasmic reticulum. J. Cell Biol. 150 (2000) 1489-1498
94. Szabadkai G., Simoni A.M., Bianchi K., De Stefani D., Leo S., Wieckowski M.R., and Rizzuto R. Mitochondrial dynamics and Ca2+ signaling. Biochim. Biophys. Acta 1763 (2006) 442-449
95. Simmen T., Aslan J.E., Blagoveshchenskaya A.D., Thomas L., Wan L., Xiang Y., Feliciangeli S.F., Hung C.H., Crump C.M., and Thomas G. Pacs-2 controls endoplasmic reticulum-mitochondria communication and bid-mediated apoptosis. EMBO J. 24 (2005) 717-729
96. Fountoulakis M., Soumaka E., Rapti K., Mavroidis M., Tsangaris G., Maris A., Weisleder N., and Capetanaki Y. Alterations in the heart mitochondrial proteome in a desmin null heart failure model. J. Mol. Cell Cardiol. 38 (2005) 461-474
97. Weisleder N., Taffet G.E., and Capetanaki Y. Bcl-2 overexpression corrects mitochondrial defects and ameliorates inherited desmin null cardiomyopathy. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 769-774
98. van der Klei I.J., Veenhuis M., and Neupert W. A morphological view on mitochondrial protein targeting. Microsc. Res. Tech. 27 (1994) 284-293
99. Brdiczka D., and Wallimann T. The importance of the outer mitochondrial compartment in regulation of energy metabolism. Mol. Cell Biochem. 133-134 (1994) 69-83
100. Fraser F., and Zammit V.A. Enrichment of carnitine palmitoyltransferases i and ii in the contact sites of rat liver mitochondria. Biochem. J. 329 Pt 2 (1998) 225-229
101. Saks V.A., Tiivel T., Kay L., Novel-Chate V., Daneshrad Z., Rossi A., Fontaine E., Keriel C., Leverve X., Ventura-Clapier R., Anflous K., Samuel J.L., and Rappaport L. On the regulation of cellular energetics in health and disease. Mol. Cell Biochem. 160-161 (1996) 195-208
102. Saks V.A., Veksler V.I., Kuznetsov A.V., Kay L., Sikk P., Tiivel T., Tranqui L., Olivares J., Winkler K., Wiedemann F., and Kunz W.S. Permeabilized cell and skinned fiber techniques in studies of mitochondrial function in vivo. Mol. Cell Biochem. 184 (1998) 81-100
103. Maloyan A., Sanbe A., Osinska H., Westfall M., Robinson D., Imahashi K., Murphy E., and Robbins J. Mitochondrial dysfunction and apoptosis underlie the pathogenic process in alpha-B-crystallin desmin-related cardiomyopathy. Circulation 112 (2005) 3451-3461
104. Linden M., Li Z., Paulin D., Gotow T., and Leterrier J.F. Effects of desmin gene knockout on mice heart mitochondria. J. Bioenerg. Biomembr. 33 (2001) 333-341
105. Linden M., and Karlsson G. Identification of Porin as a binding site for Map2. Biochem. Biophys. Res. Commun. 218 (1996) 833-836
106. Leterrier J.F., Rusakov D.A., Nelson B.D., and Linden M. Interactions between brain mitochondria and cytoskeleton: evidence for specialized outer membrane domains involved in the association of cytoskeleton-associated proteins to mitochondria in situ and in vitro. Microsc. Res. Tech. 27 (1994) 233-261
107. Reipert S., Steinbock F., Fischer I., Bittner R.E., Zeold A., and Wiche G. Association of mitochondria with plectin and desmin intermediate filaments in striated muscle. Exp. Cell Res. 252 (1999) 479-491
108. Meeusen S.L., and Nunnari J. How mitochondria fuse. Curr. Opin. Cell Biol. 17 (2005) 389-394
109. Karbowski M., and Youle R.J. Dynamics of mitochondrial morphology in healthy cells and during apoptosis. Cell Death Differ. 10 (2003) 870-880
110. Perfettini J.L., Roumier T., and Kroemer G. Mitochondrial fusion and fission in the control of apoptosis. Trends Cell Biol. 15 (2005) 179-183
111. Fritz S., Weinbach N., and Westermann B. Mdm30 is an F-Box protein required for maintenance of fusion-competent mitochondria in yeast. Mol. Biol. Cell 14 (2003) 2303-2313
112. Frederick R.L.M.J., Cunningham K.W., Okamoto K., and Shaw J.M. Yeast Micro GTPase, Gem1p, regulates mitochondrial morphology via a novel pathway. J. Cell Biol. 167 (2004) 87-98
113. Smirnova E., Griparic L., Shurl D.L., and van der Bliek A.M. Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells. Mol. Biol. Cell 12 (2001) 2245-2256
114. James D.I., Parone P.A., Mattenberger Y., and Martinou J.C. Hfis1, a novel component of the mammalian mitochondrial fission machinery. J. Biol. Chem. 278 (2003) 36373-36379
115. Katsumoto T., Inoue M., Naguro T., and Kurimura T. Association of cytoskeletons with the Golgi apparatus: three-dimensional observation and computer-graphic reconstruction. J. Electron. Microsc. (Tokyo) 40 (1991) 24-28
116. Gao Y.S., Vrielink A., MacKenzie R., and Sztul E. A novel type of regulation of the vimentin intermediate filament cytoskeleton by a Golgi protein. Eur. J. Cell Biol. 81 (2002) 391-401
117. Suzuki T., Nakamoto T., Ogawa S., Seo S., Matsumura T., Tachibana K., Morimoto C., and Hirai H. Mical, a novel Casl interacting molecule, associates with vimentin. J. Biol. Chem. 277 (2002) 14933-14941
118. Kumemura H., Harada M., Omary M.B., Sakisaka S., Suganuma T., Namba M., and Sata M. Aggregation and loss of cytokeratin filament networks inhibit Golgi organization in liver-derived epithelial cell lines. Cell Motil. Cytoskeleton 57 (2004) 37-52
119. A. Kouloumenta, M. Mavroidis, Y. Capetanaki, Proper perinuclear localization of the trim-like protein, myospryn, requires its binding partner, desmin. (Submitted for publication).
120. Kouloumenta A., Mavroidis M., and Capetanaki Y. Proper perinuclear localization of the trim-like protein myospryn requires its binding partner, desmin. Mol. Biol. Cell 17 (2006) (Suppl)
121. Li W., Zhang Q., Oiso N., Novak E.K., Gautam R., O'Brien E.P., Tinsley C.L., Blake D.J., Spritz R.A., Copeland N.G., Jenkins N.A., Amato D., Roe B.A., Starcevic M., Dell'Angelica E.C., Elliott R.W., Mishra V., Kingsmore S.F., Paylor R.E., and Swank R.T. Hermansky-Pudlak syndrome type 7 (Hps-7) results from mutant dysbindin, a member of the biogenesis of lysosome-related organelles complex 1 (Bloc-1). Nat. Genet. 35 (2003) 84-89
122. Styers M.L., Salazar G., Love R., Peden A.A., Kowalczyk A.P., and Faundez V. The endo-lysosomal sorting machinery interacts with the intermediate filament cytoskeleton. Mol. Biol. Cell 15 (2004) 5369-5382
123. Blankson H., Holen I., and Seglen P.O. Disruption of the cytokeratin cytoskeleton and inhibition of hepatocytic autophagy by okadaic acid. Exp. Cell Res. 218 (1995) 522-530
124. Holen I., Gordon P.B., and Seglen P.O. protein kinase-dependent effects of okadaic acid on hepatocytic autophagy and cytoskeletal integrity. Biochem. J. 284 Pt 3 (1992) 633-636
125. Boriek A.M., Capetanaki Y., Hwang W., Officer T., Badshah M., Rodarte J., and Tidball J.G. desmin integrates the three-dimensional mechanical properties of muscles. Am. J. Physiol.: Cell Physiol. 280 (2001) C46-C52
126. Li Q., Muragaki Y., Ueno H., and Ooshima A. Stretch-induced proliferation of cultured vascular smooth muscle cells and a possible involvement of local renin-angiotensin system and platelet-derived growth factor (Pdgf). Hypertens. Res. 20 (1997) 217-223
127. Li Z., Mericskay M., Agbulut O., Butler-Browne G., Carlsson L., Thornell L.E., Babinet C., and Paulin D. 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
128. Haubold K.W., Allen D.L., Capetanaki Y., and Leinwand L.A. Loss of desmin leads to impaired voluntary wheel running and treadmill exercise performance. J. Appl. Physiol. 95 (2003) 1617-1622
129. Goldfarb L.G., Vicart P., Goebel H.H., and Dalakas M.C. Desmin myopathy. Brain 127 (2004) 723-734
130. Raats J.M., Schaart G., Henderik J.B., van der Kemp A., Dunia I., Benedetti E.L., Pieper F.R., Ramaekers F.C., and Bloemendal H. Muscle-specific expression of a dominant negative desmin mutant in transgenic mice. Eur. J. Cell Biol. 71 (1996) 221-236
131. Sjoberg G., Saavedra-Matiz C.A., Rosen D.R., Wijsman E.M., Borg K., Horowitz S.H., and Sejersen T. A missense mutation in the desmin rod domain is associated with autosomal dominant distal myopathy, and exerts a dominant negative effect on filament formation. Hum. Mol. Genet. 8 (1999) 2191-2198
132. Bar H., Kostareva A., Sjoberg G., Sejersen T., Katus H.A., and Herrmann H. forced expression of desmin and desmin mutants in cultured cells: impact of myopathic missense mutations in the central coiled-coil domain on network formation. Exp. Cell Res. 312 (2006) 1554-1565
133. Bar H., Mucke N., Kostareva A., Sjoberg G., Aebi U., and Herrmann H. Severe muscle disease-causing desmin mutations interfere with in vitro filament assembly at distinct stages. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 15099-15104
134. Alcalai R., Metzger S., Rosenheck S., Meiner V., and Chajek-Shaul T. a recessive mutation in desmoplakin causes arrhythmogenic right ventricular dysplasia, skin disorder, and woolly hair. J. Am. Coll. Cardiol. 42 (2003) 319-327
135. Wang X., Osinska H., Dorn II G.W., Nieman M., Lorenz J.N., Gerdes A.M., Witt S., Kimball T., Gulick J., and Robbins J. Mouse model of desmin-related cardiomyopathy. Circulation 103 (2001) 2402-2407
136. Liu J., Tang M., Mestril R., and Wang X. Aberrant protein aggregation is essential for a mutant desmin to impair the proteolytic function of the ubiquitin-proteasome system in cardiomyocytes. J. Mol. Cell Cardiol. 40 (2006) 451-454
137. Bence N.F., Sampat R.M., and Kopito R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292 (2001) 1552-1555
138. Sanbe A., Osinska H., Villa C., Gulick J., Klevitsky R., Glabe C.G., Kayed R., and Robbins J. Reversal of amyloid-induced heart disease in desmin-related cardiomyopathy. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 13592-13597
139. Li Z., Colucci-Guyon E., Pincon-Raymond M., Mericskay M., Pournin S., Paulin D., and Babinet C. Cardiovascular lesions and skeletal myopathy in mice lacking desmin. Dev. Biol. 175 (1996) 362-366
140. S. Psarras, M. Mavroidis, D. Sanoudou, G. Xanthou, V. Panoutsakopoulou and Y. Capetanaki, Tissue inflammation contributes to desmin-deficient cardiomyopathy (Submitted for publication).
141. Goebel H.H. Desmin-related neuromuscular disorders. Muscle Nerve 18 (1995) 1306-1320
142. Dalakas M.C., Park K.Y., Semino-Mora C., Lee H.S., Sivakumar K., and Goldfarb L.G. Desmin myopathy, a skeletal myopathy with cardiomyopathy caused by mutations in the desmin gene. N. Engl. J. Med. 342 (2000) 770-780
143. Okamoto Y., Takashima H., Higuchi I., Matsuyama W., Suehara M., Nishihira Y., Hashiguchi A., Hirano R., Ng A.R., Nakagawa M., Izumo S., Osame M., and Arimura K. Molecular mechanism of rigid spine with muscular dystrophy type 1 caused by novel mutations of selenoprotein N gene. Neurogenetics 7 (2006) 175-183
144. Ferreiro A., Ceuterick-de Groote C., Marks J.J., Goemans N., Schreiber G., Hanefeld F., Fardeau M., Martin J.J., Goebel H.H., Richard P., Guicheney P., and Bonnemann C.G. Desmin-related myopathy with Mallory body-like inclusions is caused by mutations of the selenoprotein N gene. Ann. Neurol. 55 (2004) 676-686
145. Dusek R.L., Godsel L.M., and Green K.J. Discriminating roles of desmosomal cadherins: beyond desmosomal adhesion. J Dermatol Sci. 45 (2007) 7-21
146. Jefferson J.J., Leung C.L., and Liem R.K. Plakins: Goliaths that link cell junctions and the cytoskeleton. Nat. Rev., Mol. Cell Biol. 5 (2004) 542-553
147. Tsatsopoulou A.A., Protonotarios N.I., and McKenna W.J. Arrhythmogenic right ventricular dysplasia, a cell adhesion cardiomyopathy: insights into disease pathogenesis from preliminary genotype-phenotype assessment. Heart 92 (2006) 1720-1723
148. McKoy G., Protonotarios N., Crosby A., Tsatsopoulou A., Anastasakis A., Coonar A., Norman M., Baboonian C., Jeffery S., and McKenna W.J. Identification of a deletion in plakoglobin in arrhythmogenic right ventricular cardiomyopathy with palmoplantar keratoderma and woolly hair (Naxos disease). Lancet 355 (2000) 2119-2124
149. Uzumcu A., Norgett E.E., Dindar A., Uyguner O., Nisli K., Kayserili H., Sahin S.E., Dupont E., Severs N.J., Leigh I.M., Yuksel-Apak M., Kelsell D.P., and Wollnik B. Loss of desmoplakin isoform I causes early onset cardiomyopathy and heart failure in a Naxos-like syndrome. J. Med. Genet. 43 (2006) e5
150. Syrris P., Ward D., Asimaki A., Evans A., Sen-Chowdhry S., Hughes S.E., and McKenna W.J. Desmoglein-2 mutations in arrhythmogenic right ventricular cardiomyopathy: a genotype-phenotype characterization of familial disease. Eur Heart J. 28 (2007) 581-588
151. Wiche G. Role of plectin in cytoskeleton organization and dynamics. J. Cell Sci. 111 Pt 17 (1998) 2477-2486
152. Pfendner E., Rouan F., and Uitto J. Progress in epidermolysis bullosa: the phenotypic spectrum of plectin mutations. Exp. Dermatol. 14 (2005) 241-249
153. Schroder R., Kunz W.S., Rouan F., Pfendner E., Tolksdorf K., Kappes-Horn K., Altenschmidt-Mehring M., Knoblich R., van der Ven P.F., Reimann J., Furst D.O., Blumcke I., Vielhaber S., Zillikens D., Eming S., Klockgether T., Uitto J., Wiche G., and Rolfs A. Disorganization of the desmin cytoskeleton and mitochondrial dysfunction in plectin-related epidermolysis bullosa simplex with muscular dystrophy. J. Neuropathol. Exp. Neurol. 61 (2002) 520-530
154. Gruenbaum Y., Margalit A., Goldman R.D., Shumaker D.K., and Wilson K.L. The nuclear lamina comes of age. Nat. Rev., Mol. Cell Biol. 6 (2005) 21-31
155. Bonne G., Di Barletta M.R., Varnous S., Becane H.M., Hammouda E.H., Merlini L., Muntoni F., Greenberg C.R., Gary F., Urtizberea J.A., Duboc D., Fardeau M., Toniolo D., and Schwatz K. Mutations in the gene encoding lamin A/C cause autosomal dominant Emery-Dreifuss muscular dystrophy. Nat. Genet. 21 (1999) 285-288
156. Muchir A., Bonne G., van der Kooi A.J., van Meegen M., Baas F., Bolhuis P.A., de Visser M., and Schwartz K. Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (Lgmd1b). Hum. Mol. Genet. 9 (2000) 1453-1459
157. Fatkin D., MacRae C., Sasaki T., Wolff M.R., Porcu M., Frenneaux M., Atherton J., Vidaillet Jr. H.J., Spudich S., De Girolami U., Seidman J.G., Seidman C., Muntoni F., Muehle G., Johnson W., and McdDonough B. Missense Mutations in the Rod domain of the lamin A/C gene as causes of dilated cardiomyopathy and conduction-system disease. N. Engl. J. Med. 341 (1999) 1715-1724
158. Brodsky G.L., Muntoni F., Miocic S., Sinagra G., Sewry C., and Mestroni L. Lamin A/C gene mutation associated with dilated cardiomyopathy with variable skeletal muscle involvement. Circulation 101 (2000) 473-476
159. Burke B., and Stewart C.L. Life at the edge: the nuclear envelope and human disease. Nat. Rev., Mol. Cell Biol. 3 (2002) 575-585
160. Gotzmann J., and Foisner R. A-type lamin complexes and regenerative potential: a step towards understanding laminopathic diseases?. Histochem. Cell Biol. 125 (2006) 33-41
161. Ariza A., Coll J., Fernandez-Figueras M.T., Lopez M.D., Mate J.L., Garcia O., Fernandez-Vasalo A., and Navas-Palacios J.J. Desmin myopathy: a multisystem disorder involving skeletal, cardiac, and smooth muscle. Hum. Pathol. 26 (1995) 1032-1037
162. Abraham S.C., DeNofrio D., Loh E., Minda J.M., Tomaszewski J.E., Pietra G.G., and Reynolds C. Desmin myopathy involving cardiac, skeletal, and vascular smooth muscle: report of a case with immunoelectron microscopy. Hum. Pathol. 29 (1998) 876-882
163. Arbustini E., Pasotti M., Pilotto A., Pellegrini C., Grasso M., Previtali S., Repetto A., Bellini O., Azan G., Scaffino M., Campana C., Piccolo G., Vigano M., and Tavazzi L. Desmin accumulation restrictive cardiomyopathy and atrioventricular block associated with desmin gene defects. Eur. J. Heart Fail. 8 (2006) 477-483
164. Pruszczyk P., Kostera-Pruszczyk A., Shatunov A., Goudeau B., Draminska A., Takeda K., Sambuughin N., Vicart P., Strelkov S.V., Goldfarb L.G., and Kaminska A. Restrictive cardiomyopathy with atrioventricular conduction block resulting from a desmin mutation. Int. J. Cardiol. 117 (2006) 244-253
165. Goudeau B., Rodrigues-Lima F., Fischer D., Casteras-Simon M., Sambuughin N., de Visser M., Laforet P., Ferrer X., Chapon F., Sjoberg G., Kostareva A., Sejersen T., Dalakas M.C., Goldfarb L.G., and Vicart P. Variable pathogenic potentials of mutations located in the desmin alpha-helical domain. Hum. Mutat. 27 (2006) 906-913
166. Bar H., Fischer D., Goudeau B., Kley R.A., Clemen C.S., Vicart P., Herrmann H., Vorgerd M., and Schroder R. Pathogenic effects of a novel heterozygous R350p desmin mutation on the assembly of desmin intermediate filaments in vivo and in vitro. Hum. Mol. Genet. 14 (2005) 1251-1260
167. Fidzianska A., Kotowicz J., Sadowska M., Goudeau B., Walczak E., Vicart P., and Hausmanowa-Petrusewicz I. A novel desmin R355p mutation causes cardiac and skeletal myopathy. Neuromuscul. Disord. 15 (2005) 525-531