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Volumn 374, Issue 2, 2008, Pages 320-324

Archvillin anchors in the Z-line of skeletal muscle via the nebulin C-terminus

Author keywords

Archvillin; Costamere; Nebulin; Yeast two hybrid; Z Line

Indexed keywords

ARCHVILLIN; MUSCLE PROTEIN; NEBULIN;

EID: 48349146367     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.07.036     Document Type: Article
Times cited : (8)

References (29)
  • 2
    • 0033013812 scopus 로고    scopus 로고
    • Myofibrillogenesis in the developing chicken heart: assembly of Z-disk, M-line and the thick filaments
    • Ehler E., Rothen B.M., Hammerle S.P., Komiyama M., and Perriard J.C. Myofibrillogenesis in the developing chicken heart: assembly of Z-disk, M-line and the thick filaments. J. Cell Sci. 112 (1999) 1529-1539
    • (1999) J. Cell Sci. , vol.112 , pp. 1529-1539
    • Ehler, E.1    Rothen, B.M.2    Hammerle, S.P.3    Komiyama, M.4    Perriard, J.C.5
  • 3
    • 0034285043 scopus 로고    scopus 로고
    • To the heart of myofibril assembly
    • Gregorio C.C., and Antin P.B. To the heart of myofibril assembly. Trends Cell Biol. 10 (2000) 355-362
    • (2000) Trends Cell Biol. , vol.10 , pp. 355-362
    • Gregorio, C.C.1    Antin, P.B.2
  • 4
    • 0034776199 scopus 로고    scopus 로고
    • Telethonin and other new proteins of the Z-disc of skeletal muscle
    • Faulkner G., Lanfranchi G., and Valle G. Telethonin and other new proteins of the Z-disc of skeletal muscle. IUBMB Life 51 (2001) 275-282
    • (2001) IUBMB Life , vol.51 , pp. 275-282
    • Faulkner, G.1    Lanfranchi, G.2    Valle, G.3
  • 5
    • 0029037896 scopus 로고
    • The complete primary structure of human nebulin and its correlation to muscle structure
    • Labeit S., and Kolmerer B. The complete primary structure of human nebulin and its correlation to muscle structure. J. Mol. Biol. 248 (1995) 308-315
    • (1995) J. Mol. Biol. , vol.248 , pp. 308-315
    • Labeit, S.1    Kolmerer, B.2
  • 6
    • 0030039635 scopus 로고    scopus 로고
    • Human skeletal muscle nebulin sequence encodes a blueprint for thin filament architecture. Sequence motifs and affinity profiles of tandem repeats and terminal SH3
    • Wang K., Knipfer M., Huang Q.Q., van Heerden A., Hsu L.C., Gutierrez G., Quian X.L., and Stedman H. Human skeletal muscle nebulin sequence encodes a blueprint for thin filament architecture. Sequence motifs and affinity profiles of tandem repeats and terminal SH3. J. Biol. Chem. 271 (1996) 4304-4314
    • (1996) J. Biol. Chem. , vol.271 , pp. 4304-4314
    • Wang, K.1    Knipfer, M.2    Huang, Q.Q.3    van Heerden, A.4    Hsu, L.C.5    Gutierrez, G.6    Quian, X.L.7    Stedman, H.8
  • 7
    • 18744397819 scopus 로고    scopus 로고
    • Molecular dissection of the interaction of desmin with the C-terminal region of nebulin
    • Bang M.L., Gregorio C., and Labeit S. Molecular dissection of the interaction of desmin with the C-terminal region of nebulin. J. Struct. Biol. 137 (2002) 119-127
    • (2002) J. Struct. Biol. , vol.137 , pp. 119-127
    • Bang, M.L.1    Gregorio, C.2    Labeit, S.3
  • 9
    • 0037132502 scopus 로고    scopus 로고
    • Interaction of nebulin SH3 domain with titin PEVK and myopalladin: implications for the signaling and assembly role of titin and nebulin
    • Ma K., and Wang K. Interaction of nebulin SH3 domain with titin PEVK and myopalladin: implications for the signaling and assembly role of titin and nebulin. FEBS Lett. 532 (2002) 273-278
    • (2002) FEBS Lett. , vol.532 , pp. 273-278
    • Ma, K.1    Wang, K.2
  • 10
    • 0038348502 scopus 로고    scopus 로고
    • Archvillin, a muscle-specific isoform of supervillin, is an early expressed component of the costameric membrane skeleton
    • Oh S.W., Pope R.K., Smith K.P., Crowley J.L., Nebl T., Lawrence J.B., and Luna E.J. Archvillin, a muscle-specific isoform of supervillin, is an early expressed component of the costameric membrane skeleton. J. Cell Sci. 116 (2003) 2261-2275
    • (2003) J. Cell Sci. , vol.116 , pp. 2261-2275
    • Oh, S.W.1    Pope, R.K.2    Smith, K.P.3    Crowley, J.L.4    Nebl, T.5    Lawrence, J.B.6    Luna, E.J.7
  • 11
    • 0030831613 scopus 로고    scopus 로고
    • Supervillin (p205): a novel membrane-associated, F-actin-binding protein in the villin/gelsolin superfamily
    • Pestonjamasp K.N., Pope R.K., Wulfkuhle J.D., and Luna E.J. Supervillin (p205): a novel membrane-associated, F-actin-binding protein in the villin/gelsolin superfamily. J. Cell Biol. 139 (1997) 1255-1269
    • (1997) J. Cell Biol. , vol.139 , pp. 1255-1269
    • Pestonjamasp, K.N.1    Pope, R.K.2    Wulfkuhle, J.D.3    Luna, E.J.4
  • 13
    • 0032820201 scopus 로고    scopus 로고
    • Domain analysis of supervillin, an F-actin bundling plasma membrane protein with functional nuclear localization signals
    • Wulfkuhle J.D., Donina I.E., Stark N.H., Pope R.K., Pestonjamasp K.N., Niswonger M.L., and Luna E.J. Domain analysis of supervillin, an F-actin bundling plasma membrane protein with functional nuclear localization signals. J. Cell Sci. 112 (1999) 2125-2136
    • (1999) J. Cell Sci. , vol.112 , pp. 2125-2136
    • Wulfkuhle, J.D.1    Donina, I.E.2    Stark, N.H.3    Pope, R.K.4    Pestonjamasp, K.N.5    Niswonger, M.L.6    Luna, E.J.7
  • 15
    • 0037044851 scopus 로고    scopus 로고
    • Proteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membranes
    • Nebl T., Pestonjamasp K.N., Leszyk J.D., Crowley J.L., Oh S.W., and Luna E.J. Proteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membranes. J. Biol. Chem. 277 (2002) 43399-43409
    • (2002) J. Biol. Chem. , vol.277 , pp. 43399-43409
    • Nebl, T.1    Pestonjamasp, K.N.2    Leszyk, J.D.3    Crowley, J.L.4    Oh, S.W.5    Luna, E.J.6
  • 16
    • 0034014229 scopus 로고    scopus 로고
    • The cell and developmental biology of tendons and ligaments
    • Benjamin M., and Ralphs J.R. The cell and developmental biology of tendons and ligaments. Int. Rev. Cytol. 196 (2000) 85-130
    • (2000) Int. Rev. Cytol. , vol.196 , pp. 85-130
    • Benjamin, M.1    Ralphs, J.R.2
  • 17
    • 0031252066 scopus 로고    scopus 로고
    • Supramolecular organization of the subsarcolemmal cytoskeleton of adult skeletal muscle fibers. A review
    • Berthier C., and Blaineau S. Supramolecular organization of the subsarcolemmal cytoskeleton of adult skeletal muscle fibers. A review. Biol. Cell 89 (1997) 413-434
    • (1997) Biol. Cell , vol.89 , pp. 413-434
    • Berthier, C.1    Blaineau, S.2
  • 19
    • 0029027202 scopus 로고
    • Immunocytochemistry of the muscle cell cytoskeleton
    • Stromer M.H. Immunocytochemistry of the muscle cell cytoskeleton. Microsc. Res. Tech. 31 (1995) 95-105
    • (1995) Microsc. Res. Tech. , vol.31 , pp. 95-105
    • Stromer, M.H.1
  • 21
    • 0026739841 scopus 로고
    • Costameres are sites of force transmission to the substratum in adult rat cardiomyocytes
    • Danowski B.A., Imanaka-Yoshida K., Sanger J.M., and Sanger J.W. Costameres are sites of force transmission to the substratum in adult rat cardiomyocytes. J. Cell Biol. 118 (1992) 1411-1420
    • (1992) J. Cell Biol. , vol.118 , pp. 1411-1420
    • Danowski, B.A.1    Imanaka-Yoshida, K.2    Sanger, J.M.3    Sanger, J.W.4
  • 22
    • 0020698866 scopus 로고
    • Lateral transmission of tension in frog myofibers: a myofibrillar network and transverse cytoskeletal connections are possible transmitters
    • Street S.F. Lateral transmission of tension in frog myofibers: a myofibrillar network and transverse cytoskeletal connections are possible transmitters. J. Cell Physiol. 114 (1983) 346-364
    • (1983) J. Cell Physiol. , vol.114 , pp. 346-364
    • Street, S.F.1
  • 24
    • 0018571673 scopus 로고
    • Desmin and vimentin coexist at the periphery of the myofibril Z disc
    • Granger B.L., and Lazarides E. Desmin and vimentin coexist at the periphery of the myofibril Z disc. Cell 18 (1979) 1053-1063
    • (1979) Cell , vol.18 , pp. 1053-1063
    • Granger, B.L.1    Lazarides, E.2
  • 25
    • 0019841086 scopus 로고
    • Immunoelectron and immunofluorescence localization of desmin in mature avian muscles
    • Richardson F.L., Stromer M.H., Huiatt T.W., and Robson R.M. Immunoelectron and immunofluorescence localization of desmin in mature avian muscles. Eur. J. Cell Biol. 26 (1981) 91-101
    • (1981) Eur. J. Cell Biol. , vol.26 , pp. 91-101
    • Richardson, F.L.1    Stromer, M.H.2    Huiatt, T.W.3    Robson, R.M.4
  • 26
    • 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. Immunoelectron microscopic studies of desmin (skeletin) localization and intermediate filament organization in chicken skeletal muscle. J. Cell Biol. 96 (1983) 1727-1735
    • (1983) J. Cell Biol. , vol.96 , pp. 1727-1735
    • Tokuyasu, K.T.1    Dutton, A.H.2    Singer, S.J.3
  • 27
    • 0020960791 scopus 로고
    • Immunoelectron microscopic studies of desmin (skeletin) localization and intermediate filament organization in chicken cardiac muscle
    • Tokuyasu K.T., Dutton A.H., and Singer S.J. Immunoelectron microscopic studies of desmin (skeletin) localization and intermediate filament organization in chicken cardiac muscle. J. Cell Biol. 96 (1983) 1736-1742
    • (1983) J. Cell Biol. , vol.96 , pp. 1736-1742
    • Tokuyasu, K.T.1    Dutton, A.H.2    Singer, S.J.3
  • 28
    • 0021241389 scopus 로고
    • Immunocytochemical analysis of intermediate filaments in embryonic heart cells with monoclonal antibodies to desmin
    • Danto S.I., and Fischman D.A. Immunocytochemical analysis of intermediate filaments in embryonic heart cells with monoclonal antibodies to desmin. J. Cell Biol. 98 (1984) 2179-2191
    • (1984) J. Cell Biol. , vol.98 , pp. 2179-2191
    • Danto, S.I.1    Fischman, D.A.2
  • 29
    • 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. 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
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.