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Volumn 121, Issue 12, 2008, Pages 2062-2074

Plectin 1 links intermediate filaments to costameric sarcolemma through β-synemin, α-dystrobrevin and actin

Author keywords

Costamere; Dystrobrevin; Dystrophin glycoprotein complex; Plectin; Synemin

Indexed keywords

ACTIN; ALPHA DYSTROBREVIN; BETA SYNEMIN; DYSTROPHIN; DYSTROPHIN ASSOCIATED PROTEIN COMPLEX; INTEGRIN; INTERMEDIATE FILAMENT PROTEIN; ISOPROTEIN; PLECTIN; PLECTIN 1;

EID: 47649083199     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.021634     Document Type: Article
Times cited : (51)

References (77)
  • 1
    • 13344285342 scopus 로고    scopus 로고
    • The three human syntrophin genes are expressed in diverse tissues, have distinct chromosomal locations, and each bind to dystrophin and its relatives
    • Ahn, A. H., Freener, C. A., Gussoni, E., Yoshida, M., Ozawa, E. and Kunkel, L. M. (1996). The three human syntrophin genes are expressed in diverse tissues, have distinct chromosomal locations, and each bind to dystrophin and its relatives. J. Biol. Chem. 271, 2724-2730.
    • (1996) J. Biol. Chem , vol.271 , pp. 2724-2730
    • Ahn, A.H.1    Freener, C.A.2    Gussoni, E.3    Yoshida, M.4    Ozawa, E.5    Kunkel, L.M.6
  • 2
    • 0030721040 scopus 로고    scopus 로고
    • Targeted inactivation of plectin reveals essential finiction in maintaining the integrity of skin, muscle, and heart cytoarchitecture
    • Andra, K., Lassmann, H., Bittner, R., Shorny, S., Fassier, R., Propst, F. and Wiche, G. (1997). Targeted inactivation of plectin reveals essential finiction in maintaining the integrity of skin, muscle, and heart cytoarchitecture. Genes Dev. 11, 3143-3156.
    • (1997) Genes Dev , vol.11 , pp. 3143-3156
    • Andra, K.1    Lassmann, H.2    Bittner, R.3    Shorny, S.4    Fassier, R.5    Propst, F.6    Wiche, G.7
  • 3
    • 0032213892 scopus 로고    scopus 로고
    • Not just scaffolding: Plectin regulates actin dynamics in cultured cells
    • Andra, K., Nikolic, B., Stocher, M., Drenckhahn, D. and Wiche, G. (1998). Not just scaffolding: plectin regulates actin dynamics in cultured cells. Genev Dev. 12, 3442-3451.
    • (1998) Genev Dev , vol.12 , pp. 3442-3451
    • Andra, K.1    Nikolic, B.2    Stocher, M.3    Drenckhahn, D.4    Wiche, G.5
  • 4
    • 0344826002 scopus 로고    scopus 로고
    • Lower active force generation and improved fatigue resistance in skeletal muscle from desmin deficient mice
    • Balogh, J., Li, Z., Paulin, D. and Arner, A. (2003). Lower active force generation and improved fatigue resistance in skeletal muscle from desmin deficient mice. J. Muscle Res. Cell Motil. 24, 453-459.
    • (2003) J. Muscle Res. Cell Motil , vol.24 , pp. 453-459
    • Balogh, J.1    Li, Z.2    Paulin, D.3    Arner, A.4
  • 5
    • 0029671374 scopus 로고    scopus 로고
    • Beta ID integrin displaces the beta 1A isoform in striated muscles: Localization at junctional structures and signaling potential in nonmuscle cells
    • Belkin, A. M., Zhidkova, N. I., Balzac, F., Altruda, F., Tomatis, D, Maier, A., Tarone, G., Koteliansky, V. E. and Burridge, K. (1996). Beta ID integrin displaces the beta 1A isoform in striated muscles: localization at junctional structures and signaling potential in nonmuscle cells. J. Cell Biol. 132, 211-226.
    • (1996) J. Cell Biol , vol.132 , pp. 211-226
    • Belkin, A.M.1    Zhidkova, N.I.2    Balzac, F.3    Altruda, F.4    Tomatis, D.5    Maier, A.6    Tarone, G.7    Koteliansky, V.E.8    Burridge, K.9
  • 6
    • 0032878518 scopus 로고    scopus 로고
    • Molecular characteristics and interactions of the intermediate filament protein synemin. Interactions with alpha-actinin may anchor synemin-containing heterofilaments
    • Bellin, R. M., Sernett, S. W., Becker, B., Ip, W, Huiatt, T. W. and Robson, R. M. (1999). Molecular characteristics and interactions of the intermediate filament protein synemin. Interactions with alpha-actinin may anchor synemin-containing heterofilaments. J. Biol. Chem. 274, 29493-29499.
    • (1999) J. Biol. Chem , vol.274 , pp. 29493-29499
    • Bellin, R.M.1    Sernett, S.W.2    Becker, B.3    Ip, W.4    Huiatt, T.W.5    Robson, R.M.6
  • 7
    • 0035943673 scopus 로고    scopus 로고
    • Synemin may function to directly link muscle cell intermediate filaments to both myofibrillar Z-1ines and costameres
    • Bellin, R. M., Huiatt, T. W., Critchley, D. R. and Robson, R. M. (2001). Synemin may function to directly link muscle cell intermediate filaments to both myofibrillar Z-1ines and costameres. J. Biol. Chem. 276, 32330-32337.
    • (2001) J. Biol. Chem , vol.276 , pp. 32330-32337
    • Bellin, R.M.1    Huiatt, T.W.2    Critchley, D.R.3    Robson, R.M.4
  • 10
    • 13344277364 scopus 로고    scopus 로고
    • Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha1-syntrophin mediated by PDZ domains
    • Brenman, J. E., Chao, D. S., Gee, S. H., McGee, A. W., Craven, S. E., Sautillano, D. R., Wu, Z., Huang, F., Xia, H., Peters, M. F. et al. (1996). Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha1-syntrophin mediated by PDZ domains. Cell 84, 757-767.
    • (1996) Cell , vol.84 , pp. 757-767
    • Brenman, J.E.1    Chao, D.S.2    Gee, S.H.3    McGee, A.W.4    Craven, S.E.5    Sautillano, D.R.6    Wu, Z.7    Huang, F.8    Xia, H.9    Peters, M.F.10
  • 11
    • 0033853845 scopus 로고    scopus 로고
    • Differences in the distribution of synemin, paranemin, and plectin in skeletal muscles of wild-type and desmin knock-out mice
    • Carlsson, L., Li, Z. L., Paulin, D., Price, M. G., Breckler, J., Robson, R. M., Wiche, G. and Thornell, L. E. (2000). Differences in the distribution of synemin, paranemin, and plectin in skeletal muscles of wild-type and desmin knock-out mice. Histochem. Cell Biol. 114, 39-47.
    • (2000) Histochem. Cell Biol , vol.114 , pp. 39-47
    • Carlsson, L.1    Li, Z.L.2    Paulin, D.3    Price, M.G.4    Breckler, J.5    Robson, R.M.6    Wiche, G.7    Thornell, L.E.8
  • 12
    • 0027943989 scopus 로고
    • A human keratin 14 "knockout": The absence of K14 leads to severe epidermolysis bullosa simplex and a function for an intermediate filament protein
    • Chan, Y., Anton-Lamprecht, I., Yu, Q. C., Jäckel, A., Zabel, B, Ernst, J. P. and Fuchs, E. (1994). A human keratin 14 "knockout": the absence of K14 leads to severe epidermolysis bullosa simplex and a function for an intermediate filament protein. Genes Dev. 8, 2574-2587.
    • (1994) Genes Dev , vol.8 , pp. 2574-2587
    • Chan, Y.1    Anton-Lamprecht, I.2    Yu, Q.C.3    Jäckel, A.4    Zabel, B.5    Ernst, J.P.6    Fuchs, E.7
  • 13
    • 0021009545 scopus 로고
    • Gamma actin, spectrin, and intermediate filament proteins colocalize with vinculin at costameres, myofibril-to-sarcolemma attachment sites
    • Craig, S. W. and Pardo, J. V. (1983). Gamma actin, spectrin, and intermediate filament proteins colocalize with vinculin at costameres, myofibril-to-sarcolemma attachment sites. Cell Motil. 3, 449-462.
    • (1983) Cell Motil , vol.3 , pp. 449-462
    • Craig, S.W.1    Pardo, J.V.2
  • 14
    • 0029666420 scopus 로고    scopus 로고
    • Beta4 integrin is required for hemidesmosome formation, cell adhesion and cell survival
    • Dowling, J., Yu, Q. C. and Fuchs, E. (1996). Beta4 integrin is required for hemidesmosome formation, cell adhesion and cell survival. J. Cell Biol. 134, 559-572.
    • (1996) J. Cell Biol , vol.134 , pp. 559-572
    • Dowling, J.1    Yu, Q.C.2    Fuchs, E.3
  • 16
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti, J. M. and Campbell, K. P. (1993). A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J. Cell Biol. 122, 809-823.
    • (1993) J. Cell Biol , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 17
    • 0023840076 scopus 로고
    • Cytoskeleton-associated plectin: In situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins
    • Foisner, R., Leichtfried, F. F., Herrmann, H., Small, J. V., Lawson, D. and Wiche, G. (1988). Cytoskeleton-associated plectin: in situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins. J. Cell Biol. 106, 723-733.
    • (1988) J. Cell Biol , vol.106 , pp. 723-733
    • Foisner, R.1    Leichtfried, F.F.2    Herrmann, H.3    Small, J.V.4    Lawson, D.5    Wiche, G.6
  • 18
    • 0034953789 scopus 로고    scopus 로고
    • The interaction of plectin with actin: Evidence for cross-linking of actin filaments by dimerization of the actin-binding domain of plectin
    • Fontao, L., Geerts, D, Kuikman, I., Koster, J., Kramer, D. and Sonnenberg, A. (2001). The interaction of plectin with actin: evidence for cross-linking of actin filaments by dimerization of the actin-binding domain of plectin. J. Cell Sci. 114, 2065-2076.
    • (2001) J. Cell Sci , vol.114 , pp. 2065-2076
    • Fontao, L.1    Geerts, D.2    Kuikman, I.3    Koster, J.4    Kramer, D.5    Sonnenberg, A.6
  • 19
    • 0344462732 scopus 로고    scopus 로고
    • Unusual 5′ transcript complexity of plectin isoforms: Novel tissue-specific exons modulate actin binding activity
    • Fuchs, P., Zorer, M., Rezniczek, G. A., Spazierer, D., Oehler, S., Castanon, M. J., Hauptmann, R. and Wiche, G. (1999). Unusual 5′ transcript complexity of plectin isoforms: novel tissue-specific exons modulate actin binding activity. Hum. Mol. Genet. 8, 2461-2472.
    • (1999) Hum. Mol. Genet , vol.8 , pp. 2461-2472
    • Fuchs, P.1    Zorer, M.2    Rezniczek, G.A.3    Spazierer, D.4    Oehler, S.5    Castanon, M.J.6    Hauptmann, R.7    Wiche, G.8
  • 20
    • 0002712253 scopus 로고
    • The association of intermediate filaments with the sarcolemma in skeletal muscle fibers
    • Kyoto, p
    • Fujikamki, N., Kano, Y. and Ishikawa, H. (1986). The association of intermediate filaments with the sarcolemma in skeletal muscle fibers. In Proc XIth Int Cong on Electron Microscopy, Kyoto, p2657-2658.
    • (1986) Proc XIth Int Cong on Electron Microscopy , pp. 2657-2658
    • Fujikamki, N.1    Kano, Y.2    Ishikawa, H.3
  • 21
  • 22
    • 0032589487 scopus 로고    scopus 로고
    • Binding of integrin alpha6beta4 to plectin prevents plectin association with F-actin but does not interfere with intermediate filament binding
    • Geerts, D., Fontao, L., Nievers, M. G., Schaapveld, R. Q., Purkis, P. E., Wheeler, G. N., Lane, E. B., Leigh, I. M. and Sonnenberg, A. (1999). Binding of integrin alpha6beta4 to plectin prevents plectin association with F-actin but does not interfere with intermediate filament binding. J. Cell Biol. 147, 417-434.
    • (1999) J. Cell Biol , vol.147 , pp. 417-434
    • Geerts, D.1    Fontao, L.2    Nievers, M.G.3    Schaapveld, R.Q.4    Purkis, P.E.5    Wheeler, G.N.6    Lane, E.B.7    Leigh, I.M.8    Sonnenberg, A.9
  • 23
  • 24
    • 0019195947 scopus 로고
    • Synemin: A new high molecular weight protein associated with desmin and vimentin filaments in muscle
    • Granger, B. L. and Lazarldes, E. (1980). Synemin: a new high molecular weight protein associated with desmin and vimentin filaments in muscle. Cell 22, 727-738.
    • (1980) Cell , vol.22 , pp. 727-738
    • Granger, B.L.1    Lazarldes, E.2
  • 25
    • 0032494165 scopus 로고    scopus 로고
    • Gamma-sarcoglycan deficiency leads to muscle membrane defects and apoptosis independent of dystrophin
    • Hack, A. A., Ly, C. T., Jiang, F., Clendenin, C. J., Sigrist, K. S., Wollmann, R. L. and McNally, E. M. (1998). Gamma-sarcoglycan deficiency leads to muscle membrane defects and apoptosis independent of dystrophin. J. Cell Biol. 142, 1279-1287.
    • (1998) J. Cell Biol , vol.142 , pp. 1279-1287
    • Hack, A.A.1    Ly, C.T.2    Jiang, F.3    Clendenin, C.J.4    Sigrist, K.S.5    Wollmann, R.L.6    McNally, E.M.7
  • 26
    • 0033885496 scopus 로고    scopus 로고
    • Differential requirement for individual sarcoglycatis and dystrophin in the assembly and function of the dystrophin-glycoprotein complex
    • Hack, A. A., Lam, M. Y., Cordier, L., Shorturma, D. I., Ly, C. T., Hadhazy, M. A., Hadhazy, M. R., Sweeney, H. L. and MaNally, E. M. (2000). Differential requirement for individual sarcoglycatis and dystrophin in the assembly and function of the dystrophin-glycoprotein complex. J. Cell Sci. 113, 2535-2544.
    • (2000) J. Cell Sci , vol.113 , pp. 2535-2544
    • Hack, A.A.1    Lam, M.Y.2    Cordier, L.3    Shorturma, D.I.4    Ly, C.T.5    Hadhazy, M.A.6    Hadhazy, M.R.7    Sweeney, H.L.8    MaNally, E.M.9
  • 27
    • 33645782024 scopus 로고    scopus 로고
    • Cytoplasmic gamma-actin contributes to a compensatory remodeling response in dystrophin-deficient muscle
    • Hanft, L. M., Rybakovs, I. N., Patel, J. R., Rafael-Fortney, J. A. and Ervasti, J. M. (2006). Cytoplasmic gamma-actin contributes to a compensatory remodeling response in dystrophin-deficient muscle. Proc. Natl. Acad Sci. USA 103, 5385-5390.
    • (2006) Proc. Natl. Acad Sci. USA , vol.103 , pp. 5385-5390
    • Hanft, L.M.1    Rybakovs, I.N.2    Patel, J.R.3    Rafael-Fortney, J.A.4    Ervasti, J.M.5
  • 28
    • 0031453038 scopus 로고    scopus 로고
    • Molecular characteristics of the novel intermediate filament protein paranemin. Sequence reveals EAP-300 and IFAPa-400 are highly homologous to paranemin
    • Hemken, P. M., Bellin, R. M., Sernett, S. W., Becker, B., Huiatt, T. W. and Robson, R. M. (1997). Molecular characteristics of the novel intermediate filament protein paranemin. Sequence reveals EAP-300 and IFAPa-400 are highly homologous to paranemin. J. Biol. Chem. 272, 32499-32499.
    • (1997) J. Biol. Chem , vol.272 , pp. 32499-32499
    • Hemken, P.M.1    Bellin, R.M.2    Sernett, S.W.3    Becker, B.4    Huiatt, T.W.5    Robson, R.M.6
  • 29
    • 0026577999 scopus 로고
    • Identification of a new hemidesmosomal protein, HD1: A major, high molecular mass component of isolated hemidesmosomes
    • Hieda, Y., Nishizawa, Y., Uematsu, J. and Owaribe, K. (1992). Identification of a new hemidesmosomal protein, HD1: a major, high molecular mass component of isolated hemidesmosomes. J. Cell Biol. 116, 1497-1506.
    • (1992) J. Cell Biol , vol.116 , pp. 1497-1506
    • Hieda, Y.1    Nishizawa, Y.2    Uematsu, J.3    Owaribe, K.4
  • 30
    • 0030868453 scopus 로고    scopus 로고
    • Unanticipated temporal and spatial effects of sarcomeric alpha-actinin peptides expressed in PtK2 cells
    • Hijikata, T., Lin, Z. X., Holtzer, S., Choi, J., Sweeney, H. L. and Holtzer, H. (1997). Unanticipated temporal and spatial effects of sarcomeric alpha-actinin peptides expressed in PtK2 cells. Cell Motil. Cytoskeleton 38, 54-74.
    • (1997) Cell Motil. Cytoskeleton , vol.38 , pp. 54-74
    • Hijikata, T.1    Lin, Z.X.2    Holtzer, S.3    Choi, J.4    Sweeney, H.L.5    Holtzer, H.6
  • 31
    • 0032899830 scopus 로고    scopus 로고
    • Plectin is a linker of intermediate filaments to Z-discs in skeletal muscle fibers
    • Hijikata, T, Murakami, T., Imamura, M., Fujimaki, N. and Ishikawa, H. (1999). Plectin is a linker of intermediate filaments to Z-discs in skeletal muscle fibers. J. Cell Sci. 112, 867-876.
    • (1999) J. Cell Sci , vol.112 , pp. 867-876
    • Hijikata, T.1    Murakami, T.2    Imamura, M.3    Fujimaki, N.4    Ishikawa, H.5
  • 32
    • 0037295486 scopus 로고    scopus 로고
    • Plectin tethers desmin intermediate filaments onto subsarcolemmal dense plaques containing dystrophin and vinculin
    • Hijikata, T., Murakami, T, Ishikawa, H. and Yorifuji, H. (2003). Plectin tethers desmin intermediate filaments onto subsarcolemmal dense plaques containing dystrophin and vinculin. Histochem. Cell Biol. 119, 109-123.
    • (2003) Histochem. Cell Biol , vol.119 , pp. 109-123
    • Hijikata, T.1    Murakami, T.2    Ishikawa, H.3    Yorifuji, H.4
  • 33
    • 10744230626 scopus 로고    scopus 로고
    • Characterization of mammalian synemin, an intermediate filament protein present in all four classes of muscle cells and some neuroglial cells: Co-localization and interaction with type III intermediate filament proteins and keratins
    • Hirako, Y., Yamakawa, H., Tsujimura, Y., Nishizawa, Y., Okumura, M., Usukura, J., Matsumoto, H., Jackson, K. W., Owaribe, K. and Ohara, O. (2003). Characterization of mammalian synemin, an intermediate filament protein present in all four classes of muscle cells and some neuroglial cells: co-localization and interaction with type III intermediate filament proteins and keratins. Cell Tissue Res. 313, 195-207.
    • (2003) Cell Tissue Res , vol.313 , pp. 195-207
    • Hirako, Y.1    Yamakawa, H.2    Tsujimura, Y.3    Nishizawa, Y.4    Okumura, M.5    Usukura, J.6    Matsumoto, H.7    Jackson, K.W.8    Owaribe, K.9    Ohara, O.10
  • 34
    • 0030809116 scopus 로고    scopus 로고
    • Altered expression ofthe alpha7betal integrin in human and murine muscular dystrophies
    • Hodges, B. L., Hayashi, Y. K., Nonaka, I., Wang, W., Arahata, K. and Kaufman, S. J. (1997). Altered expression ofthe alpha7betal integrin in human and murine muscular dystrophies. J. Cell Sci. 110, 2873-2881.
    • (1997) J. Cell Sci , vol.110 , pp. 2873-2881
    • Hodges, B.L.1    Hayashi, Y.K.2    Nonaka, I.3    Wang, W.4    Arahata, K.5    Kaufman, S.J.6
  • 35
    • 0023614188 scopus 로고
    • Dystrophin: The protein product of the Duchenne muscular dystrophy locus
    • Hoffman, E. P., Brown, R. H., Jr and Kunkel, L. M. (1987). Dystrophin: the protein product of the Duchenne muscular dystrophy locus. Cell 51, 919-928.
    • (1987) Cell , vol.51 , pp. 919-928
    • Hoffman, E.P.1    Brown Jr, R.H.2    Kunkel, L.M.3
  • 36
    • 0036156170 scopus 로고    scopus 로고
    • Deletion of the cytoplasmatic domain of BP180/collagen XVII causes a phenotype with predominant features of epidermolysis bullosa simplex
    • Huber, M., Floeth, M., Borradori, L, Schäcke, H, Rugg, E. L., Lane, E. B., Frenk, E., Hohl, D. and Bruckner-Tuderman, L. (2002). Deletion of the cytoplasmatic domain of BP180/collagen XVII causes a phenotype with predominant features of epidermolysis bullosa simplex. J. Invest. Dermatol. 118, 185-192.
    • (2002) J. Invest. Dermatol , vol.118 , pp. 185-192
    • Huber, M.1    Floeth, M.2    Borradori, L.3    Schäcke, H.4    Rugg, E.L.5    Lane, E.B.6    Frenk, E.7    Hohl, D.8    Bruckner-Tuderman, L.9
  • 37
    • 0032568564 scopus 로고    scopus 로고
    • Differential expression of dystrophin isoforms and utrophin during dibutyryl-cAMP-induced morphological differentiation of rat brain astrocytes
    • Imamura, M. and Ozawa, E. (1998). Differential expression of dystrophin isoforms and utrophin during dibutyryl-cAMP-induced morphological differentiation of rat brain astrocytes. Proc. Natl. Acad. Sci. USA 95, 6139-6144.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6139-6144
    • Imamura, M.1    Ozawa, E.2
  • 38
    • 0028264218 scopus 로고
    • Talin, vinculin and DRP (utrophin) concentrations are increased at mdx myotendinous junctions following onset of necrosis
    • Law, D. J., Allen, D. L. and Tidball, J. G. (1994). Talin, vinculin and DRP (utrophin) concentrations are increased at mdx myotendinous junctions following onset of necrosis. J. Cell Sci. 107, 1477-1483.
    • (1994) J. Cell Sci , vol.107 , pp. 1477-1483
    • Law, D.J.1    Allen, D.L.2    Tidball, J.G.3
  • 39
    • 0018842868 scopus 로고
    • Intermediate filaments as mechanical integrators of cellular space
    • Lazarides, E. (1980). Intermediate filaments as mechanical integrators of cellular space. Nature 283, 249-256.
    • (1980) Nature , vol.283 , pp. 249-256
    • Lazarides, E.1
  • 41
    • 0030879081 scopus 로고    scopus 로고
    • Desmin is essential for the tensile strength and integrity of myofibrils but not for myogenic commitment, differentiation, and fusion of skeletal muscle
    • Li, Z., Mericskay, M., Agbulut, O., Butler-Browne, G., Carlsson, L., Thornell, L. E., Babinet, C. and Paulin, D. (1997). 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, 129-144.
    • (1997) J. Cell Biol , vol.139 , pp. 129-144
    • Li, Z.1    Mericskay, M.2    Agbulut, O.3    Butler-Browne, G.4    Carlsson, L.5    Thornell, L.E.6    Babinet, C.7    Paulin, D.8
  • 42
    • 33745947286 scopus 로고    scopus 로고
    • Current insights into the formation and breakdown of hemidesmosomes
    • Litjens, S. H., de Pereda, J. M. and Sonnenberg, A. (2006). Current insights into the formation and breakdown of hemidesmosomes. Trends Cell Biol. 16, 376-383.
    • (2006) Trends Cell Biol , vol.16 , pp. 376-383
    • Litjens, S.H.1    de Pereda, J.M.2    Sonnenberg, A.3
  • 43
    • 0036385851 scopus 로고    scopus 로고
    • Direct binding of plectin to Fer kiriase and negative regulation of its catalytic activity
    • Lunter, P. C. and Wiche, G. (2002). Direct binding of plectin to Fer kiriase and negative regulation of its catalytic activity. Biochem. Biophys. Res. Commun. 296, 904-910.
    • (2002) Biochem. Biophys. Res. Commun , vol.296 , pp. 904-910
    • Lunter, P.C.1    Wiche, G.2
  • 44
    • 0020538452 scopus 로고
    • Isolation and characterization of tropomyosin-containing Microfilaments from cultured cells
    • Matsumura, F., Yamashiro-Matsumura, S. and Lin, J. J. (1983). Isolation and characterization of tropomyosin-containing Microfilaments from cultured cells. J. Biol. Chem. 258, 6636-6664.
    • (1983) J. Biol. Chem , vol.258 , pp. 6636-6664
    • Matsumura, F.1    Yamashiro-Matsumura, S.2    Lin, J.J.3
  • 49
    • 10144233447 scopus 로고    scopus 로고
    • Basic amino acid residue cluster within nuclear targeting sequence motif is essential for cytoplasmic plectin-vimentin network junctions
    • Nikolic, B., Mae Nulty, E., Mir, B. and Wiche, G. (1996). Basic amino acid residue cluster within nuclear targeting sequence motif is essential for cytoplasmic plectin-vimentin network junctions. J. Cell Biol. 134, 1455-1467.
    • (1996) J. Cell Biol , vol.134 , pp. 1455-1467
    • Nikolic, B.1    Mae Nulty, E.2    Mir, B.3    Wiche, G.4
  • 50
    • 0026067790 scopus 로고
    • Dystrophin-glycoprotein complex is highly enriched in isolated skeletal muscle sarcolemma
    • Ohlendieck, K., Ervasti, J. M., Snook, J. B. and Campbell, K. P. (1991). Dystrophin-glycoprotein complex is highly enriched in isolated skeletal muscle sarcolemma. J. Cell Biol. 112, 135-148.
    • (1991) J. Cell Biol , vol.112 , pp. 135-148
    • Ohlendieck, K.1    Ervasti, J.M.2    Snook, J.B.3    Campbell, K.P.4
  • 51
    • 47649100065 scopus 로고    scopus 로고
    • The functional biology of dystrophin: Structural components and die pathogenesis of Duchenne muscular dystrophy
    • ed. J. S. Chamberlain and T. A. Rando, pp, New York, London: Taylor & Francis Group
    • Ozawa, E. (2006). The functional biology of dystrophin: structural components and die pathogenesis of Duchenne muscular dystrophy. In Duchenne Muscular Dystrophy Advances in Therapeutics (ed. J. S. Chamberlain and T. A. Rando), pp. 21-53. New York, London: Taylor & Francis Group.
    • (2006) Duchenne Muscular Dystrophy Advances in Therapeutics , pp. 21-53
    • Ozawa, E.1
  • 52
    • 0031943778 scopus 로고    scopus 로고
    • From dystrophinopathy to sarcoglycanopathy: Evolution of a concept of muscular dystrophy
    • Ozawa, E., Noguchi, S., Mizuno, Y., Hagiwara, Y. and Yoshida, M. (1998). From dystrophinopathy to sarcoglycanopathy: evolution of a concept of muscular dystrophy. Muscle Nerve 21, 421-438.
    • (1998) Muscle Nerve , vol.21 , pp. 421-438
    • Ozawa, E.1    Noguchi, S.2    Mizuno, Y.3    Hagiwara, Y.4    Yoshida, M.5
  • 55
    • 0034533580 scopus 로고    scopus 로고
    • Striated muscle-specific beta(1D)-integrin and FAK are involved in cardiac myocyte hypertrophic response pathway Am
    • Pham, C. G., Harpf, A. E., Keller, R. S., Vu, H. T., Shai, S. Y, Loftus, J. C. and Ross, R. S. (2000). Striated muscle-specific beta(1D)-integrin and FAK are involved in cardiac myocyte hypertrophic response pathway Am. J. Physiol. Heart Cire. Physiol. 279, H2916-H2926.
    • (2000) J. Physiol. Heart Cire. Physiol , vol.279
    • Pham, C.G.1    Harpf, A.E.2    Keller, R.S.3    Vu, H.T.4    Shai, S.Y.5    Loftus, J.C.6    Ross, R.S.7
  • 56
    • 0021015222 scopus 로고
    • Expression of intermediate filament-associated proteins paranemin and synemin in chicken development
    • Price, M. G. and Lazarides, E. (1983). Expression of intermediate filament-associated proteins paranemin and synemin in chicken development. J. Cell Mol. 97, 1860-1874.
    • (1983) J. Cell Mol , vol.97 , pp. 1860-1874
    • Price, M.G.1    Lazarides, E.2
  • 57
    • 0030611108 scopus 로고    scopus 로고
    • Homozygous alpha6 integrin mutation in junctional epidermolysis bullosa with congenital duodenal atresia
    • Pulkkinen, L., Kimonis, V. E., Xu, Y, Spanou, E. N, McLean, W. H. and Uitto, J. (1997). Homozygous alpha6 integrin mutation in junctional epidermolysis bullosa with congenital duodenal atresia. Hum. Mol. Genet. 6, 669-674.
    • (1997) Hum. Mol. Genet , vol.6 , pp. 669-674
    • Pulkkinen, L.1    Kimonis, V.E.2    Xu, Y.3    Spanou, E.N.4    McLean, W.H.5    Uitto, J.6
  • 58
    • 0344462724 scopus 로고    scopus 로고
    • Association of mitochondria with plectin and desmin intermediate filaments in striated muscle
    • Reipert, S., Steinbock, F., Fischer, I., Bittner, R, E., Zeold, A. and Wiche, G. (1999). Association of mitochondria with plectin and desmin intermediate filaments in striated muscle. Exp. Cell Res. 252, 479-491.
    • (1999) Exp. Cell Res , vol.252 , pp. 479-491
    • Reipert, S.1    Steinbock, F.2    Fischer, I.3    Bittner, R.E.4    Zeold, A.5    Wiche, G.6
  • 59
    • 0032489678 scopus 로고    scopus 로고
    • Linking integrin alpha6beta4-based cell adhesion to the intermediate filament cytoskeleton: Direct interaction between the beta4 subunit and plectin at multiple molecular sites
    • Rezniczek, G. A., de Pereda, J. M., Relpert, S. and Wiche, G. (1998). Linking integrin alpha6beta4-based cell adhesion to the intermediate filament cytoskeleton: direct interaction between the beta4 subunit and plectin at multiple molecular sites. J. Cell Biol. 141, 209-225.
    • (1998) J. Cell Biol , vol.141 , pp. 209-225
    • Rezniczek, G.A.1    de Pereda, J.M.2    Relpert, S.3    Wiche, G.4
  • 60
    • 0344668724 scopus 로고    scopus 로고
    • Plectin 5′-transcript diversity: Short alternative sequences determine stability of gene products, initiation of translation and subcellular localization of isoforms
    • Rezniczek G. A., Abrahamsberg, C., Fuchs, P., Spazierer, D. and Wiche, G. (2003). Plectin 5′-transcript diversity: short alternative sequences determine stability of gene products, initiation of translation and subcellular localization of isoforms. Hum. Mol. Genet. 12, 3181-3194.
    • (2003) Hum. Mol. Genet , vol.12 , pp. 3181-3194
    • Rezniczek, G.A.1    Abrahamsberg, C.2    Fuchs, P.3    Spazierer, D.4    Wiche, G.5
  • 62
    • 0034605070 scopus 로고    scopus 로고
    • The dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin
    • Rybakova, I. N., Patel, J. R. and Ervasti, J. M. (2000). The dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin. J. Cell Biol. 150, 1209-1214.
    • (2000) J. Cell Biol , vol.150 , pp. 1209-1214
    • Rybakova, I.N.1    Patel, J.R.2    Ervasti, J.M.3
  • 63
    • 0030775377 scopus 로고    scopus 로고
    • Dystrobrevin and dystrophin: An interaction through coiled-coil motifs
    • Sadoulet-Puccio, H. M., Rajala, M. and Kunkel, L. M. (1997). Dystrobrevin and dystrophin: an interaction through coiled-coil motifs. Proc. Natl. Acad. Sci. USA 94, 12413-12418.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12413-12418
    • Sadoulet-Puccio, H.M.1    Rajala, M.2    Kunkel, L.M.3
  • 64
    • 0033679588 scopus 로고    scopus 로고
    • Desmin knockout muscles generate lower stress and are less vulnerable to injury compared with wild-type muscles
    • Sam, M., Shah, S., Friden, J., Milner, D. J., Capetanaki, Y. and Lieber, R. L. (2000). Desmin knockout muscles generate lower stress and are less vulnerable to injury compared with wild-type muscles. Am. J. Physiol. Cell Physiol. 279, C1116-C1122.
    • (2000) Am. J. Physiol. Cell Physiol , vol.279
    • Sam, M.1    Shah, S.2    Friden, J.3    Milner, D.J.4    Capetanaki, Y.5    Lieber, R.L.6
  • 67
    • 0036401583 scopus 로고    scopus 로고
    • Primary longitudinal adhesion structures: Plectin-containing precursors of costameres in differentiating human skeletal muscle cells
    • Schröder, R., Pacholsky, D., Reimann, J., Matten, J., Wiche, G., Forst, D. O. and van der Ven, P. F. (2002). Primary longitudinal adhesion structures: plectin-containing precursors of costameres in differentiating human skeletal muscle cells. Histochem. Cell Biol. 118, 301-310.
    • (2002) Histochem. Cell Biol , vol.118 , pp. 301-310
    • Schröder, R.1    Pacholsky, D.2    Reimann, J.3    Matten, J.4    Wiche, G.5    Forst, D.O.6    van der Ven, P.F.7
  • 69
    • 2442675099 scopus 로고    scopus 로고
    • Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin
    • Sevcík J., Urbániková, L., Kost'an, J., Janda, L. and Wiche, G. (2004). Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin. Eur. J. Biochem. 271, 1873-1884.
    • (2004) Eur. J. Biochem , vol.271 , pp. 1873-1884
    • Sevcík, J.1    Urbániková, L.2    Kost'an, J.3    Janda, L.4    Wiche, G.5
  • 70
    • 0030909575 scopus 로고    scopus 로고
    • Muscular dystrophies and the dystrophin-glycoprotein complex
    • Straub, V. and Campbell, K. P. (1997). Muscular dystrophies and the dystrophin-glycoprotein complex. Curr. Opin. Neurol. 10, 168-175.
    • (1997) Curr. Opin. Neurol , vol.10 , pp. 168-175
    • Straub, V.1    Campbell, K.P.2
  • 71
    • 0035660405 scopus 로고    scopus 로고
    • Human synemin gene generates splice variants encoding two distinct intermediate filament proteins
    • Titeux, M., Brocheriou, V., Xue, Z., Gao, J., Pellissier, J. F., Guicheney, P., Paulin, D. and Li, Z. (2001). Human synemin gene generates splice variants encoding two distinct intermediate filament proteins. Eur. J. Biochem. 268, 6435-6449.
    • (2001) Eur. J. Biochem , vol.268 , pp. 6435-6449
    • Titeux, M.1    Brocheriou, V.2    Xue, Z.3    Gao, J.4    Pellissier, J.F.5    Guicheney, P.6    Paulin, D.7    Li, Z.8
  • 72
    • 0020955372 scopus 로고
    • Immunoelectron microscopic studies of desmin (skeletin) localization and intermediate filament organization in chicken skeletal muscle
    • Tokuyasu, K. T., Dutton, A. H. and Singer, S. J. (1983). Immunoelectron microscopic studies of desmin (skeletin) localization and intermediate filament organization in chicken skeletal muscle. J. Cell Biol. 96, 1727-1735.
    • (1983) J. Cell Biol , vol.96 , pp. 1727-1735
    • Tokuyasu, K.T.1    Dutton, A.H.2    Singer, S.J.3
  • 73
    • 0030015434 scopus 로고    scopus 로고
    • Epithelial detachment due to absence of hemidesmosomes in integrin beta 4 null mice
    • van der Neut, R., Krimpenfort, P., Calafat, J., Niessen, C. M. and Sonnenberg, A. (1996). Epithelial detachment due to absence of hemidesmosomes in integrin beta 4 null mice. Nat. Genet. 13, 366-369.
    • (1996) Nat. Genet , vol.13 , pp. 366-369
    • van der Neut, R.1    Krimpenfort, P.2    Calafat, J.3    Niessen, C.M.4    Sonnenberg, A.5
  • 75
    • 3843052495 scopus 로고    scopus 로고
    • Comparative biochemical analysis suggests that vinculin and metavinculin cooperate in muscular adhesion sites
    • Witt, S., Zieseniss, A., Fock, U., Jockusch, B. M. and Illenberger, S. (2004). Comparative biochemical analysis suggests that vinculin and metavinculin cooperate in muscular adhesion sites. J. Biol. Chem. 279, 31533-31543.
    • (2004) J. Biol. Chem , vol.279 , pp. 31533-31543
    • Witt, S.1    Zieseniss, A.2    Fock, U.3    Jockusch, B.M.4    Illenberger, S.5
  • 76
    • 0028302369 scopus 로고
    • Dissociation of the complex of dystrophin and its associated proteins into several unique groups by n-octyl beta-D-glucoside
    • Yoshida, M., Suzuki, A., Yamamoto, H., Noguchi, S., Mizano, Y. and Ozawa, E. (1994). Dissociation of the complex of dystrophin and its associated proteins into several unique groups by n-octyl beta-D-glucoside. Eur. J. Biochem. 222, 1055-1061.
    • (1994) Eur. J. Biochem , vol.222 , pp. 1055-1061
    • Yoshida, M.1    Suzuki, A.2    Yamamoto, H.3    Noguchi, S.4    Mizano, Y.5    Ozawa, E.6


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