메뉴 건너뛰기




Volumn 445, Issue 3, 2012, Pages 323-332

p130Cas-dependent actin remodelling regulates myogenic differentiation

Author keywords

Actin dynamics; Cofilin; Crk associated substrate (p130Cas); Integrin; Megakaryocytic acute leukaemia (MAL); Myogenic differentiation

Indexed keywords

ACTIN; BETA3 INTEGRIN; COFILIN; CRK ASSOCIATED SUBSTRATE PROTEIN; F ACTIN; MYOGENIC FACTOR; SERUM RESPONSE FACTOR;

EID: 84864370385     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20112169     Document Type: Article
Times cited : (24)

References (48)
  • 5
    • 0034528405 scopus 로고    scopus 로고
    • Myogenic differentiation requires signalling through both phosphatidylinositol 3-kinase and p38 MAP kinase
    • DOI 10.1016/S0898-6568(00)00120-0, PII S0898656800001200
    • Li, Y., Jiang, B., Ensign, W. Y., Vogt, P. K. and Han, J. (2000) Myogenic differentiation requires signalling through both phosphatidylinositol 3-kinase and p38 MAP kinase. Cell. Signaling 12, 751-757 (Pubitemid 32056343)
    • (2000) Cellular Signalling , vol.12 , Issue.11-12 , pp. 751-757
    • Li, Y.1    Jiang, B.-H.2    Ensign Jr., W.Y.3    Vogt, P.K.4    Han, J.5
  • 7
    • 0038586412 scopus 로고    scopus 로고
    • MyoD distal regulatory region contains an SRF binding CArG element required for MyoD expression in skeletal myoblasts and during muscle regeneration
    • DOI 10.1091/mbc.E02-07-0451
    • L'Honore, A., Lamb, N. J., Vandromme, M., Turowski, P., Carnac, G. and Fernandez, A. (2003) MyoD distal regulatory region contains an SRF binding CArG element required for MyoD expression in skeletal myoblasts and during muscle regeneration. Mol. Biol. Cell 14, 2151-2162 (Pubitemid 36583560)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.5 , pp. 2151-2162
    • L'Honore, A.1    Lamb, N.J.2    Vandromme, M.3    Turowski, P.4    Carnac, G.5    Fernandez, A.6
  • 8
    • 33745152386 scopus 로고    scopus 로고
    • The myocardin family of transcriptional coactivators: Versatile regulators of cell growth, migration, and myogenesis
    • DOI 10.1101/gad.1428006
    • Pipes, G. C., Creemers, E. E. and Olson, E. N. (2006) The myocardin family of transcriptional coactivators: versatile regulators of cell growth, migration, and myogenesis. Genes Dev. 20, 1545-1556 (Pubitemid 43901093)
    • (2006) Genes and Development , vol.20 , Issue.12 , pp. 1545-1556
    • Pipes, G.C.T.1    Creemers, E.E.2    Olson, E.N.3
  • 10
    • 33750343214 scopus 로고    scopus 로고
    • Actin' together: serum response factor, its cofactors and the link to signal transduction
    • DOI 10.1016/j.tcb.2006.09.008, PII S0962892406002698
    • Posern, G. and Treisman, R. (2006) Actin' together: serum response factor, its cofactors and the link to signal transduction. Trends Cell Biol. 16, 588-596 (Pubitemid 44636222)
    • (2006) Trends in Cell Biology , vol.16 , Issue.11 , pp. 588-596
    • Posern, G.1    Treisman, R.2
  • 11
    • 34250794416 scopus 로고    scopus 로고
    • Nuclear actin as choreographer of cell morphology and transcription
    • DOI 10.1126/science.1145014
    • Wu, J. I. and Crabtree, G. R. (2007) Cell signaling: nuclear actin as choreographer of cell morphology and transcription. Science 316, 1710-1711 (Pubitemid 46988537)
    • (2007) Science , vol.316 , Issue.5832 , pp. 1710-1711
    • Wu, J.I.1    Crabtree, G.R.2
  • 12
    • 0030722189 scopus 로고    scopus 로고
    • Regulation of distinct stages of skeletal muscle differentiation by mitogen-activated protein kinases
    • DOI 10.1126/science.278.5341.1288
    • Bennett, A. M. and Tonks, N. K. (1997) Regulation of distinct stages of skeletal muscle differentiation by mitogen-activated protein kinases. Science 278, 1288-1291 (Pubitemid 27495740)
    • (1997) Science , vol.278 , Issue.5341 , pp. 1288-1291
    • Bennett, A.M.1    Tonks, N.K.2
  • 13
    • 12844269689 scopus 로고    scopus 로고
    • Myocardin/MKL family of SRF coactivators: Key regulators of immediate early and muscle specific gene expression
    • Cen, B., Selvaraj, A. and Prywes, R. (2004) Myocardin/MKL family of SRF coactivators: key regulators of immediate early and muscle specific gene expression. J. Cell. Biochem. 93, 74-82
    • (2004) J. Cell. Biochem. , vol.93 , pp. 74-82
    • Cen, B.1    Selvaraj, A.2    Prywes, R.3
  • 14
    • 33646557326 scopus 로고    scopus 로고
    • p130Cas: A versatile scaffold in signaling networks
    • DOI 10.1016/j.tcb.2006.03.003, PII S0962892406000833
    • Defilippi, P., Di Stefano, P. and Cabodi, S. (2006) p130Cas: a versatile scaffold in signaling networks. Trends Cell Biol. 16, 257-263 (Pubitemid 43728873)
    • (2006) Trends in Cell Biology , vol.16 , Issue.5 , pp. 257-263
    • Defilippi, P.1    Di, S.P.2    Cabodi, S.3
  • 16
    • 7744232293 scopus 로고    scopus 로고
    • Activation of a signaling cascade by cytoskeleton stretch
    • DOI 10.1016/j.devcel.2004.08.021, PII S1534580704003375
    • Tamada, M., Sheetz, M. P. and Sawada, Y. (2004) Activation of a signaling cascade by cytoskeleton stretch. Dev. Cell 7, 709-718 (Pubitemid 39462691)
    • (2004) Developmental Cell , vol.7 , Issue.5 , pp. 709-718
    • Tamada, M.1    Sheetz, M.P.2    Sawada, Y.3
  • 17
    • 33751335857 scopus 로고    scopus 로고
    • Force Sensing by Mechanical Extension of the Src Family Kinase Substrate p130Cas
    • DOI 10.1016/j.cell.2006.09.044, PII S009286740601405X
    • Sawada, Y., Tamada, M., Dubin-Thaler, B. J., Cherniavskaya, O., Sakai, R., Tanaka, S. and Sheetz, M. P. (2006) Force sensing by mechanical extension of the Src family kinase substrate p130Cas. Cell 127, 1015-1026 (Pubitemid 44803062)
    • (2006) Cell , vol.127 , Issue.5 , pp. 1015-1026
    • Sawada, Y.1    Tamada, M.2    Dubin-Thaler, B.J.3    Cherniavskaya, O.4    Sakai, R.5    Tanaka, S.6    Sheetz, M.P.7
  • 19
    • 77955580383 scopus 로고    scopus 로고
    • Stretchy proteins on stretchy substrates: The important elements of integrin-mediated rigidity sensing
    • Moore, S. W., Roca-Cusachs, P. and Sheetz, M. P. (2010) Stretchy proteins on stretchy substrates: the important elements of integrin-mediated rigidity sensing. Dev. Cell 19, 194-206
    • (2010) Dev. Cell , vol.19 , pp. 194-206
    • Moore, S.W.1    Roca-Cusachs, P.2    Sheetz, M.P.3
  • 20
    • 79957912435 scopus 로고    scopus 로고
    • β3-integrin mediates satellite cell differentiation in regenerating mouse muscle
    • Liu, H., Niu, A., Chen, S. E. and Li, Y. P. (2011) β3-integrin mediates satellite cell differentiation in regenerating mouse muscle. FASEB J. 25, 1914-1921
    • (2011) FASEB J. , vol.25 , pp. 1914-1921
    • Liu, H.1    Niu, A.2    Chen, S.E.3    Li, Y.P.4
  • 21
    • 0037178809 scopus 로고    scopus 로고
    • Differential regulation of cell migration, actin stress fiber organization, and cell transformation by functional domains of Crk-associated substrate
    • DOI 10.1074/jbc.M203063200
    • Huang, J., Hamasaki, H., Nakamoto, T., Honda, H., Hirai, H., Saito, M., Takato, T. and Sakai, R. (2002) Differential regulation of cell migration, actin stress fiber organization, and cell transformation by functional domains of Crk-associated substrate. J. Biol. Chem. 277, 27265-27272 (Pubitemid 34951744)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.30 , pp. 27265-27272
    • Huang, J.1    Hamasaki, H.2    Nakamoto, T.3    Honda, H.4    Hirai, H.5    Saito, M.6    Takato, T.7    Sakai, R.8
  • 22
    • 50249145697 scopus 로고    scopus 로고
    • uPAR promotes formation of the p130Cas-Crk complex to activate Rac through DOCK180
    • Smith, H. W., Marra, P. and Marshall, C. J. (2008) uPAR promotes formation of the p130Cas-Crk complex to activate Rac through DOCK180. J. Cell Biol. 182, 777-790
    • (2008) J. Cell Biol. , vol.182 , pp. 777-790
    • Smith, H.W.1    Marra, P.2    Marshall, C.J.3
  • 23
    • 43049139541 scopus 로고    scopus 로고
    • p53 regulates glucose metabolism through an IKK-NF-κB pathway and inhibits cell transformation
    • DOI 10.1038/ncb1724, PII NCB1724
    • Kawauchi, K., Araki, K., Tobiume, K. and Tanaka, N. (2008) p53 regulates glucose metabolism through an IKK-NF-κB pathway and inhibits cell transformation. Nat. Cell Biol. 10, 611-618 (Pubitemid 351627381)
    • (2008) Nature Cell Biology , vol.10 , Issue.5 , pp. 611-618
    • Kawauchi, K.1    Araki, K.2    Tobiume, K.3    Tanaka, N.4
  • 25
    • 34248226275 scopus 로고    scopus 로고
    • αvβ3 and α5β1 integrin recycling pathways dictate downstream Rho kinase signaling to regulate persistent cell migration
    • DOI 10.1083/jcb.200609004
    • White, D. P., Caswell, P. T. and Norman, J. C. (2007) αvβ3 and α5β1 integrin recycling pathways dictate downstream Rho kinase signaling to regulate persistent cell migration. J. Cell Biol. 177, 515-525 (Pubitemid 46718279)
    • (2007) Journal of Cell Biology , vol.177 , Issue.3 , pp. 515-525
    • White, D.P.1    Caswell, P.T.2    Norman, J.C.3
  • 26
    • 53349090308 scopus 로고    scopus 로고
    • Mechanical forces facilitate actin polymerization at focal adhesions in a zyxin-dependent manner
    • Hirata, H., Tatsumi, H. and Sokabe, M. (2008) Mechanical forces facilitate actin polymerization at focal adhesions in a zyxin-dependent manner. J. Cell Sci. 121, 2795-2804
    • (2008) J. Cell Sci. , vol.121 , pp. 2795-2804
    • Hirata, H.1    Tatsumi, H.2    Sokabe, M.3
  • 27
    • 0037044198 scopus 로고    scopus 로고
    • In-gel kinase assay as a method to identify kinase substrates
    • Wooten, M. W. (2002) In-gel kinase assay as a method to identify kinase substrates. Sci. STKE 2002, pl15
    • (2002) Sci. STKE , vol.2002
    • Wooten, M.W.1
  • 28
    • 0036688904 scopus 로고    scopus 로고
    • PKC-regulated myogenesis is associated with increased tyrosine phosphorylation of FAK, Cas, and paxillin, formation of Cas-CRK complex, and JNK activation
    • DOI 10.1046/j.1432-0436.2002.700604.x
    • Goel, H. L. and Dey, C. S. (2002) PKC-regulated myogenesis is associated with increased tyrosine phosphorylation of FAK, Cas, and paxillin, formation of Cas-CRK complex, and JNK activation. Differentiation 70, 257-271 (Pubitemid 38230544)
    • (2002) Differentiation , vol.70 , Issue.6 , pp. 257-271
    • Goel, H.L.1    Dey, C.S.2
  • 29
    • 77951582061 scopus 로고    scopus 로고
    • Linking actin dynamics and gene transcription to drive cellular motile functions
    • Olson, E. N. and Nordheim, A. (2010) Linking actin dynamics and gene transcription to drive cellular motile functions. Nat. Rev. Mol. Cell Biol. 11, 353-365
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 353-365
    • Olson, E.N.1    Nordheim, A.2
  • 30
    • 77950859278 scopus 로고    scopus 로고
    • ADF/cofilin: A functional node in cell biology
    • Bernstein, B. W. and Bamburg, J. R. (2010) ADF/cofilin: a functional node in cell biology. Trends Cell Biol. 20, 187-195
    • (2010) Trends Cell Biol. , vol.20 , pp. 187-195
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 31
    • 44349149912 scopus 로고    scopus 로고
    • Cell adhesion-dependent cofilin serine 3 phosphorylation by the integrin-linked kinase· c-Src complex
    • Kim, Y. B., Choi, S., Choi, M. C., Oh, M. A., Lee, S. A., Cho, M., Mizuno, K., Kim, S. H. and Lee, J. W. (2008) Cell adhesion-dependent cofilin serine 3 phosphorylation by the integrin-linked kinase· c-Src complex. J. Biol. Chem. 283, 10089-10096
    • (2008) J. Biol. Chem. , vol.283 , pp. 10089-10096
    • Kim, Y.B.1    Choi, S.2    Choi, M.C.3    Oh, M.A.4    Lee, S.A.5    Cho, M.6    Mizuno, K.7    Kim, S.H.8    Lee, J.W.9
  • 33
    • 0035903099 scopus 로고    scopus 로고
    • Cofilin Phosphorylation and Actin Reorganization Activities of Testicular Protein Kinase 2 and Its Predominant Expression in Testicular Sertoli Cells
    • DOI 10.1074/jbc.M102988200
    • Toshima, J., Toshima, J. Y., Takeuchi, K., Mori, R. and Mizuno, K. (2001) Cofilin phosphorylation and actin reorganization activities of testicular protein kinase 2 and its predominant expression in testicular Sertoli cells. J. Biol. Chem. 276, 31449-31458 (Pubitemid 37385018)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.33 , pp. 31449-31458
    • Toshima, J.1    Toshima, J.Y.2    Takeuchi, K.3    Mori, R.4    Mizuno, K.5
  • 34
    • 80055062698 scopus 로고    scopus 로고
    • Integrin-linked kinase: Not so 'pseudo' after all
    • Hannigan, G. E., McDonald, P. C., Walsh, M. P. and Dedhar, S. (2011) Integrin-linked kinase: not so 'pseudo' after all. Oncogene 30, 4375-4385
    • (2011) Oncogene , vol.30 , pp. 4375-4385
    • Hannigan, G.E.1    McDonald, P.C.2    Walsh, M.P.3    Dedhar, S.4
  • 35
    • 0026657069 scopus 로고
    • Displacement of BrdUrd-induced YY1 by serum response factor activates skeletal α-actin transcription in embryonic myoblasts
    • Lee, T. C., Shi, Y. and Schwartz, R. J. (1992) Displacement of BrdUrd-induced YY1 by serum response factor activates skeletal α-actin transcription in embryonic myoblasts. Proc. Natl. Acad. Sci. U.S.A. 89, 9814-9818
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 9814-9818
    • Lee, T.C.1    Shi, Y.2    Schwartz, R.J.3
  • 38
    • 22544485397 scopus 로고    scopus 로고
    • The Rho family of small GTPases: Crucial regulators of skeletal myogenesis
    • DOI 10.1007/s00018-005-5029-z
    • Bryan, B. A., Li, D., Wu, X. and Liu, M. (2005) The Rho family of small GTPases: crucial regulators of skeletal myogenesis. Cell. Mol. Life Sci. 62, 1547-1555 (Pubitemid 41021578)
    • (2005) Cellular and Molecular Life Sciences , vol.62 , Issue.14 , pp. 1547-1555
    • Bryan, B.A.1    Li, D.2    Wu, X.3    Liu, M.4
  • 39
    • 34248227301 scopus 로고    scopus 로고
    • Cofilin promotes stimulus-induced lamellipodium formation by generating an abundant supply of actin monomers
    • DOI 10.1083/jcb.200610005
    • Kiuchi, T., Ohashi, K., Kurita, S. and Mizuno, K. (2007) Cofilin promotes stimulus-induced lamellipodium formation by generating an abundant supply of actin monomers. J. Cell Biol. 177, 465-476 (Pubitemid 46718275)
    • (2007) Journal of Cell Biology , vol.177 , Issue.3 , pp. 465-476
    • Kiuchi, T.1    Ohashi, K.2    Kurita, S.3    Mizuno, K.4
  • 40
    • 77954243855 scopus 로고    scopus 로고
    • Actin and serum response factor transduce physical cues from the microenvironment to regulate epidermal stem cell fate decisions
    • Connelly, J. T., Gautrot, J. E., Trappmann, B., Tan, D. W., Donati, G., Huck, W. T. and Watt, F. M. (2010) Actin and serum response factor transduce physical cues from the microenvironment to regulate epidermal stem cell fate decisions. Nat. Cell Biol. 12, 711-718
    • (2010) Nat. Cell Biol. , vol.12 , pp. 711-718
    • Connelly, J.T.1    Gautrot, J.E.2    Trappmann, B.3    Tan, D.W.4    Donati, G.5    Huck, W.T.6    Watt, F.M.7
  • 41
    • 0038737042 scopus 로고    scopus 로고
    • Actin dynamics control SRF activity by regulation of its coactivator MAL
    • DOI 10.1016/S0092-8674(03)00278-2
    • Miralles, F., Posern, G., Zaromytidou, A. I. and Treisman, R. (2003) Actin dynamics control SRF activity by regulation of its coactivator MAL. Cell 113, 329-342 (Pubitemid 36556115)
    • (2003) Cell , vol.113 , Issue.3 , pp. 329-342
    • Miralles, F.1    Posern, G.2    Zaromytidou, A.-I.3    Treisman, R.4
  • 42
    • 75049085759 scopus 로고    scopus 로고
    • The ILK/PINCH/parvin complex: The kinase is dead, long live the pseudokinase!
    • Wickstrom, S. A., Lange, A., Montanez, E. and Fassler, R. (2009) The ILK/PINCH/parvin complex: the kinase is dead, long live the pseudokinase! EMBO J. 29, 281-291
    • (2009) EMBO J. , vol.29 , pp. 281-291
    • Wickstrom, S.A.1    Lange, A.2    Montanez, E.3    Fassler, R.4
  • 43
    • 48249112975 scopus 로고    scopus 로고
    • Kindlin-2 is required for myocyte elongation and is essential for myogenesis
    • Dowling, J. J., Vreede, A. P., Kim, S., Golden, J. and Feldman, E. L. (2008) Kindlin-2 is required for myocyte elongation and is essential for myogenesis. BMC Cell Biol. 9, 36
    • (2008) BMC Cell Biol. , vol.9 , pp. 36
    • Dowling, J.J.1    Vreede, A.P.2    Kim, S.3    Golden, J.4    Feldman, E.L.5
  • 44
    • 0034698755 scopus 로고    scopus 로고
    • The roles of integrin-linked kinase in the regulation of myogenic differentiation
    • Huang, Y., Li, J., Zhang, Y. and Wu, C. (2000) The roles of integrin-linked kinase in the regulation of myogenic differentiation. J. Cell Biol. 150, 861-872
    • (2000) J. Cell Biol. , vol.150 , pp. 861-872
    • Huang, Y.1    Li, J.2    Zhang, Y.3    Wu, C.4
  • 45
    • 38349004559 scopus 로고    scopus 로고
    • Deletion of integrin-linked kinase from skeletal muscles of mice resembles muscular dystrophy due to α7β1-integrin deficiency
    • Gheyara, A. L., Vallejo-Illarramendi, A., Zang, K., Mei, L., St-Arnaud, R., Dedhar, S. and Reichardt, L. F. (2007) Deletion of integrin-linked kinase from skeletal muscles of mice resembles muscular dystrophy due to α7β1-integrin deficiency. Am. J. Pathol. 171, 1966-1977
    • (2007) Am. J. Pathol. , vol.171 , pp. 1966-1977
    • Gheyara, A.L.1    Vallejo-Illarramendi, A.2    Zang, K.3    Mei, L.4    St-Arnaud, R.5    Dedhar, S.6    Reichardt, L.F.7
  • 46
    • 33748278519 scopus 로고    scopus 로고
    • Targeted ablation of ILK from the murine heart results in dilated cardiomyopathy and spontaneous heart failure
    • DOI 10.1101/gad.1458906
    • White, D. E., Coutu, P., Shi, Y. F., Tardif, J. C., Nattel, S., St Arnaud, R., Dedhar, S. and Muller, W. J. (2006) Targeted ablation of ILK from the murine heart results in dilated cardiomyopathy and spontaneous heart failure. Genes Dev. 20, 2355-2360 (Pubitemid 44320384)
    • (2006) Genes and Development , vol.20 , Issue.17 , pp. 2355-2360
    • White, D.E.1    Coutu, P.2    Shi, Y.-F.3    Tardif, J.-C.4    Nattel, S.5    St., A.R.6    Dedhar, S.7    Muller, W.J.8
  • 47
    • 0037076211 scopus 로고    scopus 로고
    • C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes
    • Mackinnon, A. C., Qadota, H., Norman, K. R., Moerman, D. G. and Williams, B. D. (2002) C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes. Curr. Biol. 12, 787-797
    • (2002) Curr. Biol. , vol.12 , pp. 787-797
    • Mackinnon, A.C.1    Qadota, H.2    Norman, K.R.3    Moerman, D.G.4    Williams, B.D.5
  • 48
    • 33747152561 scopus 로고    scopus 로고
    • Matrix Elasticity Directs Stem Cell Lineage Specification
    • DOI 10.1016/j.cell.2006.06.044, PII S0092867406009615
    • Engler, A. J., Sen, S., Sweeney, H. L. and Discher, D. E. (2006) Matrix elasticity directs stem cell lineage specification. Cell 126, 677-689 (Pubitemid 44233625)
    • (2006) Cell , vol.126 , Issue.4 , pp. 677-689
    • Engler, A.J.1    Sen, S.2    Sweeney, H.L.3    Discher, D.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.