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Volumn 361, Issue 1, 2012, Pages 79-89

Filamin C plays an essential role in the maintenance of the structural integrity of cardiac and skeletal muscles, revealed by the medaka mutant zacro

Author keywords

Cardiac muscle; Filamin C; Medaka mutant; Skeletal muscle; Zacro

Indexed keywords

ACTIN; FILAMIN; FILAMIN C; GAMMA ACTIN; UNCLASSIFIED DRUG;

EID: 83055180637     PISSN: 00121606     EISSN: 1095564X     Source Type: Journal    
DOI: 10.1016/j.ydbio.2011.10.008     Document Type: Article
Times cited : (84)

References (78)
  • 3
    • 2342456308 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay: terminating erroneous gene expression
    • Baker K.E., Parker R. Nonsense-mediated mRNA decay: terminating erroneous gene expression. Curr. Opin. Cell Biol. 2004, 16:293-299.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 293-299
    • Baker, K.E.1    Parker, R.2
  • 4
    • 0027433289 scopus 로고
    • Alpha 7 beta 1 integrin is a component of the myotendinous junction on skeletal muscle
    • Bao Z.Z., Lakonishok M., Kaufman S., Horwitz A.F. Alpha 7 beta 1 integrin is a component of the myotendinous junction on skeletal muscle. J. Cell Sci. 1993, 106:579-589.
    • (1993) J. Cell Sci. , vol.106 , pp. 579-589
    • Bao, Z.Z.1    Lakonishok, M.2    Kaufman, S.3    Horwitz, A.F.4
  • 7
    • 8344250882 scopus 로고    scopus 로고
    • Membrane ruffles in cell migration: indicators of inefficient lamellipodia adhesion and compartments of actin filament reorganization
    • Borm B., Requardt R.P., Herzog V., Kirfel G. Membrane ruffles in cell migration: indicators of inefficient lamellipodia adhesion and compartments of actin filament reorganization. Exp. Cell Res. 2005, 302:83-95.
    • (2005) Exp. Cell Res. , vol.302 , pp. 83-95
    • Borm, B.1    Requardt, R.P.2    Herzog, V.3    Kirfel, G.4
  • 8
    • 0032588041 scopus 로고    scopus 로고
    • The alpha7beta1 integrin in muscle development and disease
    • Burkin D.J., Kaufman S.J. The alpha7beta1 integrin in muscle development and disease. Cell Tissue Res. 1999, 296:183-190.
    • (1999) Cell Tissue Res. , vol.296 , pp. 183-190
    • Burkin, D.J.1    Kaufman, S.J.2
  • 9
    • 0028914964 scopus 로고
    • Three muscular dystrophies: loss of cytoskeleton-extracellular matrix linkage
    • Campbell K.P. Three muscular dystrophies: loss of cytoskeleton-extracellular matrix linkage. Cell 1995, 80:675-679.
    • (1995) Cell , vol.80 , pp. 675-679
    • Campbell, K.P.1
  • 11
    • 0347362783 scopus 로고    scopus 로고
    • Regulation of tension-induced mechanotranscriptional signals by the microtubule network in fibroblasts
    • D'Addario M., Arora P.D., Ellen R.P., McCulloch C.A. Regulation of tension-induced mechanotranscriptional signals by the microtubule network in fibroblasts. J. Biol. Chem. 2003, 278:53090-53097.
    • (2003) J. Biol. Chem. , vol.278 , pp. 53090-53097
    • D'Addario, M.1    Arora, P.D.2    Ellen, R.P.3    McCulloch, C.A.4
  • 12
    • 0035943713 scopus 로고    scopus 로고
    • Cytoprotection against mechanical forces delivered through beta 1 integrins requires induction of filamin A
    • D'Addario M., Arora P.D., Fan J., Ganss B., Ellen R.P., McCulloch C.A. Cytoprotection against mechanical forces delivered through beta 1 integrins requires induction of filamin A. J. Biol. Chem. 2001, 276:31969-31977.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31969-31977
    • D'Addario, M.1    Arora, P.D.2    Fan, J.3    Ganss, B.4    Ellen, R.P.5    McCulloch, C.A.6
  • 13
    • 33747753150 scopus 로고    scopus 로고
    • Loss of filaminC (FLNc) results in severe defects in myogenesis and myotube structure
    • Dalkilic I., Schienda J., Thompson T.G., Kunkel L.M. Loss of filaminC (FLNc) results in severe defects in myogenesis and myotube structure. Mol. Cell. Biol. 2006, 26:6522-6534.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 6522-6534
    • Dalkilic, I.1    Schienda, J.2    Thompson, T.G.3    Kunkel, L.M.4
  • 15
    • 0038190993 scopus 로고    scopus 로고
    • Costameres: the Achilles' heel of Herculean muscle
    • Ervasti J.M. Costameres: the Achilles' heel of Herculean muscle. J. Biol. Chem. 2003, 278:13591-13594.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13591-13594
    • Ervasti, J.M.1
  • 17
    • 7944237936 scopus 로고    scopus 로고
    • The many faces of filamin: a versatile molecular scaffold for cell motility and signalling
    • Feng Y., Walsh C.A. The many faces of filamin: a versatile molecular scaffold for cell motility and signalling. Nat. Cell Biol. 2004, 6:1034-1038.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1034-1038
    • Feng, Y.1    Walsh, C.A.2
  • 18
    • 24944550989 scopus 로고    scopus 로고
    • The Z-disc proteins myotilin and FATZ-1 interact with each other and are connected to the sarcolemma via muscle-specific filamins
    • Gontier Y., Taivainen A., Fontao L., Sonnenberg A., van der Flier A., Carpen O., Faulkner G., Borradori L. The Z-disc proteins myotilin and FATZ-1 interact with each other and are connected to the sarcolemma via muscle-specific filamins. J. Cell Sci. 2005, 118:3739-3749.
    • (2005) J. Cell Sci. , vol.118 , pp. 3739-3749
    • Gontier, Y.1    Taivainen, A.2    Fontao, L.3    Sonnenberg, A.4    van der Flier, A.5    Carpen, O.6    Faulkner, G.7    Borradori, L.8
  • 23
    • 0016787774 scopus 로고
    • Isolation and properties of actin, myosin, and a new actinbinding protein in rabbit alveolar macrophages
    • Hartwig J.H., Stossel T.P. Isolation and properties of actin, myosin, and a new actinbinding protein in rabbit alveolar macrophages. J. Biol. Chem. 1975, 250:5696-5705.
    • (1975) J. Biol. Chem. , vol.250 , pp. 5696-5705
    • Hartwig, J.H.1    Stossel, T.P.2
  • 26
    • 0023614188 scopus 로고
    • Dystrophin: the protein product of the Duchenne muscular dystrophy locus
    • Hoffman E.P., Brown R.H., Kunkel L.M. Dystrophin: the protein product of the Duchenne muscular dystrophy locus. Cell 1987, 51:919-928.
    • (1987) Cell , vol.51 , pp. 919-928
    • Hoffman, E.P.1    Brown, R.H.2    Kunkel, L.M.3
  • 27
    • 0001534691 scopus 로고
    • Establishment of inbred strains of the teleost, Oryzias latipes
    • Hyodo-Taguchi Y. Establishment of inbred strains of the teleost, Oryzias latipes. Zool. Mag. 1980, 89:283-301.
    • (1980) Zool. Mag. , vol.89 , pp. 283-301
    • Hyodo-Taguchi, Y.1
  • 28
    • 0028862762 scopus 로고
    • Temporal and spatial patterns of gene expression for the hatching enzyme in the teleost embryo, Oryzias latipes
    • Inohaya K., Yasumasu S., Ishimaru M., Ohyama A., Iuchi I., Yamagami K. Temporal and spatial patterns of gene expression for the hatching enzyme in the teleost embryo, Oryzias latipes. Dev. Biol. 1995, 171:374-385.
    • (1995) Dev. Biol. , vol.171 , pp. 374-385
    • Inohaya, K.1    Yasumasu, S.2    Ishimaru, M.3    Ohyama, A.4    Iuchi, I.5    Yamagami, K.6
  • 29
    • 0032716197 scopus 로고    scopus 로고
    • Analysis of the origin and development of hatching gland cells by transplantation of the embryonic shield in the fish, Oryzias latipes
    • Inohaya K., Yasumasu S., Yasumasu I., Iuchi I., Yamagami K. Analysis of the origin and development of hatching gland cells by transplantation of the embryonic shield in the fish, Oryzias latipes. Dev. Growth Differ. 1999, 41:557-566.
    • (1999) Dev. Growth Differ. , vol.41 , pp. 557-566
    • Inohaya, K.1    Yasumasu, S.2    Yasumasu, I.3    Iuchi, I.4    Yamagami, K.5
  • 31
    • 0029919669 scopus 로고    scopus 로고
    • A recessive lethal mutation, tb, that bends the midbrain region of the neural tube in the early embryo of the medaka
    • Ishikawa Y. A recessive lethal mutation, tb, that bends the midbrain region of the neural tube in the early embryo of the medaka. Neurosci. Res. 1996, 24:313-317.
    • (1996) Neurosci. Res. , vol.24 , pp. 313-317
    • Ishikawa, Y.1
  • 32
    • 0034020820 scopus 로고    scopus 로고
    • Medakafish as a model system for vertebrate developmental genetics
    • Ishikawa Y. Medakafish as a model system for vertebrate developmental genetics. Bioessays 2000, 22:487-495.
    • (2000) Bioessays , vol.22 , pp. 487-495
    • Ishikawa, Y.1
  • 34
    • 3042631471 scopus 로고    scopus 로고
    • Stages of normal development in the medaka Oryzias latipes
    • Iwamatsu T. Stages of normal development in the medaka Oryzias latipes. Mech. Dev. 2004, 121:605-618.
    • (2004) Mech. Dev. , vol.121 , pp. 605-618
    • Iwamatsu, T.1
  • 35
    • 0037077244 scopus 로고    scopus 로고
    • Cell death and mechanoprotection by filamin A in connective tissues after challenge by applied tensile forces
    • Kainulainen T., Pender A., D'Addario M., Feng Y., Lekic P., McCulloch C.A. Cell death and mechanoprotection by filamin A in connective tissues after challenge by applied tensile forces. J. Biol. Chem. 2002, 277:21998-22009.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21998-22009
    • Kainulainen, T.1    Pender, A.2    D'Addario, M.3    Feng, Y.4    Lekic, P.5    McCulloch, C.A.6
  • 41
    • 0032483459 scopus 로고    scopus 로고
    • Filamin binds to the cytoplasmic domain of the beta1-integrin. Identification of amino acids responsible for this interaction
    • Loo D.T., Kanner S.B., Aruffo A. Filamin binds to the cytoplasmic domain of the beta1-integrin. Identification of amino acids responsible for this interaction. J. Biol. Chem. 1998, 273:23304-23312.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23304-23312
    • Loo, D.T.1    Kanner, S.B.2    Aruffo, A.3
  • 42
    • 34447296195 scopus 로고    scopus 로고
    • The pathomechanism of filaminopathy: altered biochemical properties explain the cellular phenotype of a protein aggregation myopathy
    • Lowe T., Kley R.A., van der Ven P.F., Himmel M., Huebner A., Vorgerd M., Furst D.O. The pathomechanism of filaminopathy: altered biochemical properties explain the cellular phenotype of a protein aggregation myopathy. Hum. Mol. Genet. 2007, 16:1351-1358.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 1351-1358
    • Lowe, T.1    Kley, R.A.2    van der Ven, P.F.3    Himmel, M.4    Huebner, A.5    Vorgerd, M.6    Furst, D.O.7
  • 43
    • 77953121676 scopus 로고    scopus 로고
    • A novel heterozygous deletion-insertion mutation (2695-2712 del/GTTTGT ins) in exon 18 of the filamin C gene causes filaminopathy in a large Chinese family
    • Luan X., Hong D., Zhang W., Wang Z., Yuan Y. A novel heterozygous deletion-insertion mutation (2695-2712 del/GTTTGT ins) in exon 18 of the filamin C gene causes filaminopathy in a large Chinese family. Neuromuscul. Disord. 2010, 20:390-396.
    • (2010) Neuromuscul. Disord. , vol.20 , pp. 390-396
    • Luan, X.1    Hong, D.2    Zhang, W.3    Wang, Z.4    Yuan, Y.5
  • 44
    • 0038158092 scopus 로고    scopus 로고
    • Integrins: redundant or important players in skeletal muscle?
    • Mayer U. Integrins: redundant or important players in skeletal muscle?. J. Biol. Chem. 2003, 278:14587-14590.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14587-14590
    • Mayer, U.1
  • 46
    • 0033372459 scopus 로고    scopus 로고
    • Organization of the myotendinous junction is dependent on the presence of alpha7beta1 integrin
    • Miosge N., Klenczar C., Herken R., Willem M., Mayer U. Organization of the myotendinous junction is dependent on the presence of alpha7beta1 integrin. Lab. Invest. 1999, 79:1591-1599.
    • (1999) Lab. Invest. , vol.79 , pp. 1591-1599
    • Miosge, N.1    Klenczar, C.2    Herken, R.3    Willem, M.4    Mayer, U.5
  • 52
    • 23044473461 scopus 로고    scopus 로고
    • Chicken gizzard filamin, retina filamin and cgABP260 are respectively, smooth muscle-, non-muscle- and pan-muscle-type isoforms: distribution and localization in muscles
    • Ohashi K., Oshima K., Tachikawa M., Morikawa N., Hashimoto Y., Ito M., Mori H., Kuribayashi T., Terasaki A.G. Chicken gizzard filamin, retina filamin and cgABP260 are respectively, smooth muscle-, non-muscle- and pan-muscle-type isoforms: distribution and localization in muscles. Cell Motil. Cytoskeleton 2005, 61:214-225.
    • (2005) Cell Motil. Cytoskeleton , vol.61 , pp. 214-225
    • Ohashi, K.1    Oshima, K.2    Tachikawa, M.3    Morikawa, N.4    Hashimoto, Y.5    Ito, M.6    Mori, H.7    Kuribayashi, T.8    Terasaki, A.G.9
  • 53
    • 43449130018 scopus 로고    scopus 로고
    • Zebrafish integrin-linked kinase is required in skeletal muscles for strengthening the integrin-ECM adhesion complex
    • Postel R., Vakeel P., Topczewski J., Knoll R., Bakkers J. Zebrafish integrin-linked kinase is required in skeletal muscles for strengthening the integrin-ECM adhesion complex. Dev. Biol. 2008, 318:92-101.
    • (2008) Dev. Biol. , vol.318 , pp. 92-101
    • Postel, R.1    Vakeel, P.2    Topczewski, J.3    Knoll, R.4    Bakkers, J.5
  • 56
    • 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., Ervasti J.M. The dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin. J. Cell Biol. 2000, 150:1209-1214.
    • (2000) J. Cell Biol. , vol.150 , pp. 1209-1214
    • Rybakova, I.N.1    Patel, J.R.2    Ervasti, J.M.3
  • 57
    • 0025368276 scopus 로고
    • Immunocytochemical study of dystrophin at the myotendinous junction
    • Samitt C.E., Bonilla E. Immunocytochemical study of dystrophin at the myotendinous junction. Muscle Nerve 1990, 13:493-500.
    • (1990) Muscle Nerve , vol.13 , pp. 493-500
    • Samitt, C.E.1    Bonilla, E.2
  • 59
    • 53549117700 scopus 로고    scopus 로고
    • Myofibrillar myopathies
    • Selcen D. Myofibrillar myopathies. Curr. Opin. Neurol. 2008, 21:585-589.
    • (2008) Curr. Opin. Neurol. , vol.21 , pp. 585-589
    • Selcen, D.1
  • 60
    • 0742305818 scopus 로고    scopus 로고
    • Myofibrillar myopathy: clinical, morphological and genetic studies in 63 patients
    • Selcen D., Ohno K., Engel A.G. Myofibrillar myopathy: clinical, morphological and genetic studies in 63 patients. Brain 2004, 127:439-451.
    • (2004) Brain , vol.127 , pp. 439-451
    • Selcen, D.1    Ohno, K.2    Engel, A.G.3
  • 63
    • 0024824291 scopus 로고
    • Dense immunostainings on both neuromuscular and myotendon junction with an anti-dystrophin monoclonal antibody
    • Shimizu T., Matsumura K., Sunada Y., Mannen T. Dense immunostainings on both neuromuscular and myotendon junction with an anti-dystrophin monoclonal antibody. Biomed. Res. 1989, 10:405-409.
    • (1989) Biomed. Res. , vol.10 , pp. 405-409
    • Shimizu, T.1    Matsumura, K.2    Sunada, Y.3    Mannen, T.4
  • 66
    • 0016767817 scopus 로고
    • 2+-adenosine triphosphatase requires a cofactor for activation by actin
    • 2+-adenosine triphosphatase requires a cofactor for activation by actin. J. Biol. Chem. 1975, 250:5706-5712.
    • (1975) J. Biol. Chem. , vol.250 , pp. 5706-5712
    • Stossel, T.P.1    Hartwig, J.H.2
  • 71
    • 0033952929 scopus 로고    scopus 로고
    • Characterization of muscle filamin isoforms suggests a possible role of gamma-filamin/ABP-L in sarcomeric Z-disc formation
    • van der Ven P.F., Obermann W.M., Lemke B., Gautel M., Weber K., Furst D.O. Characterization of muscle filamin isoforms suggests a possible role of gamma-filamin/ABP-L in sarcomeric Z-disc formation. Cell Motil. Cytoskeleton 2000, 45:149-162.
    • (2000) Cell Motil. Cytoskeleton , vol.45 , pp. 149-162
    • van der Ven, P.F.1    Obermann, W.M.2    Lemke, B.3    Gautel, M.4    Weber, K.5    Furst, D.O.6
  • 74
    • 0032371504 scopus 로고    scopus 로고
    • Sex-linked inheritance of the lf locus in the medaka fish (Oryzias latipes)
    • Wada H., Shimada A., Fukamachi S., Naruse K., Shima A. Sex-linked inheritance of the lf locus in the medaka fish (Oryzias latipes). Zoolog. Sci. 1998, 15:123-126.
    • (1998) Zoolog. Sci. , vol.15 , pp. 123-126
    • Wada, H.1    Shimada, A.2    Fukamachi, S.3    Naruse, K.4    Shima, A.5
  • 75
    • 0024300196 scopus 로고
    • Immunoelectron microscopic localization of dystrophin in myofibres
    • Watkins S.C., Hoffman E.P., Slayter H.S., Kunkel L.M. Immunoelectron microscopic localization of dystrophin in myofibres. Nature 1988, 333:863-866.
    • (1988) Nature , vol.333 , pp. 863-866
    • Watkins, S.C.1    Hoffman, E.P.2    Slayter, H.S.3    Kunkel, L.M.4


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