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Volumn 6, Issue 272, 2013, Pages

Signaling mechanisms in mammalian myoblast fusion

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CATENIN; BETA CATENIN; BETA1 INTEGRIN; CALCINEURIN; CAVEOLIN 3; CELL PROTEIN; FOCAL ADHESION KINASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 4; INTERLEUKIN 4 RECEPTOR; KRUPPEL LIKE FACTOR 2; KRUPPEL LIKE FACTOR 4; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE 7; MITOGEN ACTIVATED PROTEIN KINASE P38; MYOD PROTEIN; PROTEIN CDC42; PROTEIN KINASE C THETA; RAC1 PROTEIN; RAC2 PROTEIN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; STRESS ACTIVATED PROTEIN KINASE; TRANSCRIPTION FACTOR NFAT; TRANSCRIPTION FACTOR NFATC2; UNCLASSIFIED DRUG; VASCULAR CELL ADHESION MOLECULE 1; WNT PROTEIN;

EID: 84876827016     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2003832     Document Type: Review
Times cited : (171)

References (84)
  • 1
    • 84856141914 scopus 로고    scopus 로고
    • Myoblast fusion: Lessons from flies and mice
    • S. M. Abmayr, G. K. Pavlath, Myoblast fusion: Lessons from flies and mice. Development 139, 641-656 (2012).
    • (2012) Development , vol.139 , pp. 641-656
    • Abmayr, S.M.1    Pavlath, G.K.2
  • 2
    • 77951213472 scopus 로고    scopus 로고
    • Myoblast fusion: When it takes more to make one
    • K. Rochlin, S. Yu, S. Roy, M. K. Baylies, Myoblast fusion: When it takes more to make one. Dev. Biol. 341, 66-83 (2010).
    • (2010) Dev. Biol. , vol.341 , pp. 66-83
    • Rochlin, K.1    Yu, S.2    Roy, S.3    Baylies, M.K.4
  • 3
    • 77957662730 scopus 로고    scopus 로고
    • Spatial and functional restriction of regulatory molecules during mammalian myoblast fusion
    • G. K. Pavlath, Spatial and functional restriction of regulatory molecules during mammalian myoblast fusion. Exp. Cell Res. 316, 3067-3072 (2010).
    • (2010) Exp. Cell Res. , vol.316 , pp. 3067-3072
    • Pavlath, G.K.1
  • 4
    • 77957680199 scopus 로고    scopus 로고
    • Regulation of promyogenic signal transduction by cell-cell contact and adhesion
    • R. S. Krauss, Regulation of promyogenic signal transduction by cell-cell contact and adhesion. Exp. Cell Res. 316, 3042-3049 (2010).
    • (2010) Exp. Cell Res. , vol.316 , pp. 3042-3049
    • Krauss, R.S.1
  • 6
    • 77951184829 scopus 로고    scopus 로고
    • Cellular functions of FAK kinases: Insight into molecular mechanisms and novel functions
    • M. D. Schaller, Cellular functions of FAK kinases: Insight into molecular mechanisms and novel functions. J. Cell Sci. 123, 1007-1013 (2010).
    • (2010) J. Cell Sci. , vol.123 , pp. 1007-1013
    • Schaller, M.D.1
  • 7
    • 67749101848 scopus 로고    scopus 로고
    • Focal adhesion kinase signaling regulates the expression of caveolin 3 and beta1 integrin, genes essential for normal myoblast fusion
    • N. L. Quach, S. Biressi, L. F. Reichardt, C. Keller, T. A. Rando, Focal adhesion kinase signaling regulates the expression of caveolin 3 and beta1 integrin, genes essential for normal myoblast fusion. Mol. Biol. Cell 20, 3422-3435 (2009).
    • (2009) Mol. Biol. Cell , vol.20 , pp. 3422-3435
    • Quach, N.L.1    Biressi, S.2    Reichardt, L.F.3    Keller, C.4    Rando, T.A.5
  • 8
    • 79954602263 scopus 로고    scopus 로고
    • PKCθ signaling is required for myoblast fusion by regulating the expression of caveolin-3 and β1D integrin upstream focal adhesion kinase
    • L. Madaro, V. Marrocco, P. Fiore, P. Aulino, P. Smeriglio, S. Adamo, M. Molinaro, M. Bouché, PKCθ signaling is required for myoblast fusion by regulating the expression of caveolin-3 and β1D integrin upstream focal adhesion kinase. Mol. Biol. Cell 22, 1409-1419 (2011).
    • (2011) Mol. Biol. Cell , vol.22 , pp. 1409-1419
    • Madaro, L.1    Marrocco, V.2    Fiore, P.3    Aulino, P.4    Smeriglio, P.5    Adamo, S.6    Molinaro, M.7    Bouché, M.8
  • 9
    • 48749108701 scopus 로고    scopus 로고
    • Emerging roles for neogenin and its ligands in CNS development
    • M. De Vries, H. M. Cooper, Emerging roles for neogenin and its ligands in CNS development. J. Neurochem. 106, 1483-1492 (2008).
    • (2008) J. Neurochem. , vol.106 , pp. 1483-1492
    • De Vries, M.1    Cooper, H.M.2
  • 10
    • 73949157930 scopus 로고    scopus 로고
    • Neogenin regulates skeletal myofiber size and focal adhesion kinase and extracellular signal-regulated kinase activities in vivo and in vitro
    • G. U. Bae, Y. J. Yang, G. Jiang, M. Hong, H. J. Lee, M. Tessier-Lavigne, J. S. Kang, R. S. Krauss, Neogenin regulates skeletal myofiber size and focal adhesion kinase and extracellular signal-regulated kinase activities in vivo and in vitro. Mol. Biol. Cell 20, 4920-4931 (2009).
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4920-4931
    • Bae, G.U.1    Yang, Y.J.2    Jiang, G.3    Hong, M.4    Lee, H.J.5    Tessier-Lavigne, M.6    Kang, J.S.7    Krauss, R.S.8
  • 12
    • 12344250987 scopus 로고    scopus 로고
    • Focal adhesion kinase is not required for integrin function or viability in Drosophila
    • C. Grabbe, C. G. Zervas, T. Hunter, N. H. Brown, R. H. Palmer, Focal adhesion kinase is not required for integrin function or viability in Drosophila. Development 131, 5795-5805 (2004).
    • (2004) Development , vol.131 , pp. 5795-5805
    • Grabbe, C.1    Zervas, C.G.2    Hunter, T.3    Brown, N.H.4    Palmer, R.H.5
  • 13
    • 0017759258 scopus 로고
    • Serial passaging and differentiation of myogenic cells isolated from dystrophic mouse muscle
    • D. Yaffe, O. Saxel, Serial passaging and differentiation of myogenic cells isolated from dystrophic mouse muscle. Nature 270, 725-727 (1977).
    • (1977) Nature , vol.270 , pp. 725-727
    • Yaffe, D.1    Saxel, O.2
  • 14
    • 0020960766 scopus 로고
    • Cytoplasmic activation of human nuclear genes in stable heterocaryons
    • H. M. Blau, C. P. Chiu, C. Webster, Cytoplasmic activation of human nuclear genes in stable heterocaryons. Cell 32, 1171-1180 (1983).
    • (1983) Cell , vol.32 , pp. 1171-1180
    • Blau, H.M.1    Chiu, C.P.2    Webster, C.3
  • 15
    • 0033836513 scopus 로고    scopus 로고
    • Critical activities of Rac1 and Cdc42Hs in skeletal myogenesis: Antagonistic effects of JNK and p38 pathways
    • M. Meriane, P. Roux, M. Primig, P. Fort, C. Gauthier-Rouvière, Critical activities of Rac1 and Cdc42Hs in skeletal myogenesis: Antagonistic effects of JNK and p38 pathways. Mol. Biol. Cell 11, 2513-2528 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2513-2528
    • Meriane, M.1    Roux, P.2    Primig, M.3    Fort, P.4    Gauthier-Rouvière, C.5
  • 16
    • 0037009074 scopus 로고    scopus 로고
    • N-cadherin-dependent cell-cell contact regulates Rho GTPases and beta-catenin localization in mouse C2C12 myoblasts
    • S. Charrasse, M. Meriane, F. Comunale, A. Blangy, C. Gauthier- Rouvière, N-cadherin-dependent cell-cell contact regulates Rho GTPases and beta-catenin localization in mouse C2C12 myoblasts. J. Cell Biol. 158, 953-965 (2002).
    • (2002) J. Cell Biol. , vol.158 , pp. 953-965
    • Charrasse, S.1    Meriane, M.2    Comunale, F.3    Blangy, A.4    Gauthier-Rouvière, C.5
  • 17
    • 51049114512 scopus 로고    scopus 로고
    • Rho/ Rho-associated kinase signal regulates myogenic differentiation via myocardin-related transcription factor-A/Smad-dependent transcription of the Id3 gene
    • K. Iwasaki, K. Hayashi, T. Fujioka, K. Sobue, Rho/ Rho-associated kinase signal regulates myogenic differentiation via myocardin-related transcription factor-A/Smad-dependent transcription of the Id3 gene. J. Biol. Chem. 283, 21230-21241 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 21230-21241
    • Iwasaki, K.1    Hayashi, K.2    Fujioka, T.3    Sobue, K.4
  • 18
    • 49749125994 scopus 로고    scopus 로고
    • A Cdo-Bnip-2-Cdc42 signaling pathway regulates p38alpha/beta MAPK activity and myogenic differentiation
    • J. S. Kang, G. U. Bae, M. J. Yi, Y. J. Yang, J. E. Oh, G. Takaesu, Y. T. Zhou, B. C. Low, R. S. Krauss, A Cdo-Bnip-2-Cdc42 signaling pathway regulates p38alpha/beta MAPK activity and myogenic differentiation. J. Cell Biol. 182, 497-507 (2008).
    • (2008) J. Cell Biol. , vol.182 , pp. 497-507
    • Kang, J.S.1    Bae, G.U.2    Yi, M.J.3    Yang, Y.J.4    Oh, J.E.5    Takaesu, G.6    Zhou, Y.T.7    Low, B.C.8    Krauss, R.S.9
  • 19
    • 22544485397 scopus 로고    scopus 로고
    • The Rho family of small GTPases: Crucial regulators of skeletal myogenesis
    • B. A. Bryan, D. Li, X. Wu, M. Liu, The Rho family of small GTPases: Crucial regulators of skeletal myogenesis. Cell. Mol. Life Sci. 62, 1547-1555 (2005).
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 1547-1555
    • Bryan, B.A.1    Li, D.2    Wu, X.3    Liu, M.4
  • 23
    • 79960388670 scopus 로고    scopus 로고
    • Skeletal muscle differentiation and fusion are regulated by the BAR-containing Rho-GTPase-activating protein (Rho-GAP), GRAF1
    • J. T. Doherty, K. C. Lenhart, M. V. Cameron, C. P. Mack, F. L. Conlon, J. M. Taylor, Skeletal muscle differentiation and fusion are regulated by the BAR-containing Rho-GTPase-activating protein (Rho-GAP), GRAF1. J. Biol. Chem. 286, 25903- 25921 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 25903-25921
    • Doherty, J.T.1    Lenhart, K.C.2    Cameron, M.V.3    Mack, C.P.4    Conlon, F.L.5    Taylor, J.M.6
  • 26
    • 0028980059 scopus 로고
    • Mutations in a novel gene, myoblast city, provide evidence in support of the founder cell hypothesis for Drosophila muscle development
    • E. Rushton, R. Drysdale, S. M. Abmayr, A. M. Michelson, M. Bate, Mutations in a novel gene, myoblast city, provide evidence in support of the founder cell hypothesis for Drosophila muscle development. Development 121, 1979-1988 (1995).
    • (1995) Development , vol.121 , pp. 1979-1988
    • Rushton, E.1    Drysdale, R.2    Abmayr, S.M.3    Michelson, A.M.4    Bate, M.5
  • 27
    • 0030816709 scopus 로고    scopus 로고
    • Drosophila myoblast city encodes a conserved protein that is essential for myoblast fusion, dorsal closure, and cytoskeletal organization
    • M. R. Erickson, B. J. Galletta, S. M. Abmayr, Drosophila myoblast city encodes a conserved protein that is essential for myoblast fusion, dorsal closure, and cytoskeletal organization. J. Cell Biol. 138, 589-603 (1997).
    • (1997) J. Cell Biol. , vol.138 , pp. 589-603
    • Erickson, M.R.1    Galletta, B.J.2    Abmayr, S.M.3
  • 28
    • 0032213953 scopus 로고    scopus 로고
    • Myoblast city, the Drosophila homolog of DOCK180/CED-5, is required in a Rac signaling pathway utilized for multiple developmental processes
    • K. M. Nolan, K. Barrett, Y. Lu, K. Q. Hu, S. Vincent, J. Settleman, Myoblast city, the Drosophila homolog of DOCK180/CED-5, is required in a Rac signaling pathway utilized for multiple developmental processes. Genes Dev. 12, 3337-3342 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 3337-3342
    • Nolan, K.M.1    Barrett, K.2    Lu, Y.3    Hu, K.Q.4    Vincent, S.5    Settleman, J.6
  • 29
    • 0037115488 scopus 로고    scopus 로고
    • Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity
    • J. F. Côté, K. Vuori, Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity. J. Cell Sci. 115, 4901-4913 (2002).
    • (2002) J. Cell Sci. , vol.115 , pp. 4901-4913
    • Côté, J.F.1    Vuori, K.2
  • 30
    • 34848897173 scopus 로고    scopus 로고
    • A role for the Myoblast city homologues Dock1 and Dock5 and the adaptor proteins Crk and Crk-like in zebrafish myoblast fusion
    • C. A. Moore, C. A. Parkin, Y. Bidet, P. W. Ingham, A role for the Myoblast city homologues Dock1 and Dock5 and the adaptor proteins Crk and Crk-like in zebrafish myoblast fusion. Development 134, 3145-3153 (2007).
    • (2007) Development , vol.134 , pp. 3145-3153
    • Moore, C.A.1    Parkin, C.A.2    Bidet, Y.3    Ingham, P.W.4
  • 34
    • 0035282334 scopus 로고    scopus 로고
    • Mammalian MAP kinase signalling cascades
    • L. Chang, M. Karin, Mammalian MAP kinase signalling cascades. Nature 410, 37-40 (2001).
    • (2001) Nature , vol.410 , pp. 37-40
    • Chang, L.1    Karin, M.2
  • 37
    • 77949892208 scopus 로고    scopus 로고
    • Transforming growth factor-beta-activated kinase 1 is an essential regulator of myogenic differentiation
    • S. Bhatnagar, A. Kumar, D. Y. Makonchuk, H. Li, A. Kumar, Transforming growth factor-beta-activated kinase 1 is an essential regulator of myogenic differentiation. J. Biol. Chem. 285, 6401-6411 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 6401-6411
    • Bhatnagar, S.1    Kumar, A.2    Makonchuk, D.Y.3    Li, H.4    Kumar, A.5
  • 38
    • 0035203194 scopus 로고    scopus 로고
    • ERK1/2 is required for myoblast proliferation but is dispensable for muscle gene expression and cell fusion
    • N. C. Jones, Y. V. Fedorov, R. S. Rosenthal, B. B. Olwin, ERK1/2 is required for myoblast proliferation but is dispensable for muscle gene expression and cell fusion. J. Cell. Physiol. 186, 104- 115 (2001).
    • (2001) J. Cell. Physiol. , vol.186 , pp. 104-115
    • Jones, N.C.1    Fedorov, Y.V.2    Rosenthal, R.S.3    Olwin, B.B.4
  • 39
    • 0035958008 scopus 로고    scopus 로고
    • Critical proliferation-independent window for basic fibroblast growth factor repression of myogenesis via the p42/p44 MAPK signaling pathway
    • L. L. Tortorella, D. J. Milasincic, P. F. Pilch, Critical proliferation-independent window for basic fibroblast growth factor repression of myogenesis via the p42/p44 MAPK signaling pathway. J. Biol. Chem. 276, 13709-13717 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 13709-13717
    • Tortorella, L.L.1    Milasincic, D.J.2    Pilch, P.F.3
  • 40
    • 0032562574 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathway is involved in the differentiation of muscle cells
    • E. Gredinger, A. N. Gerber, Y. Tamir, S. J. Tapscott, E. Bengal, Mitogen-activated protein kinase pathway is involved in the differentiation of muscle cells. J. Biol. Chem. 273, 10436-10444 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 10436-10444
    • Gredinger, E.1    Gerber, A.N.2    Tamir, Y.3    Tapscott, S.J.4    Bengal, E.5
  • 41
    • 0034769309 scopus 로고    scopus 로고
    • Extracellular signal regulated kinase 5 (ERK5) is required for the differentiation of muscle cells
    • D. Dinev, B. W. Jordan, B. Neufeld, J. D. Lee, D. Lindemann, U. R. Rapp, S. Ludwig, Extracellular signal regulated kinase 5 (ERK5) is required for the differentiation of muscle cells. EMBO Rep. 2, 829-834 (2001).
    • (2001) EMBO Rep. , vol.2 , pp. 829-834
    • Dinev, D.1    Jordan, B.W.2    Neufeld, B.3    Lee, J.D.4    Lindemann, D.5    Rapp, U.R.6    Ludwig, S.7
  • 43
    • 0035939662 scopus 로고    scopus 로고
    • Identification and characterization of a novel extracellular matrix protein nephronectin that is associated with integrin alpha8beta1 in the embryonic kidney
    • R. Brandenberger, A. Schmidt, J. Linton, D. Wang, C. Backus, S. Denda, U. Müller, L. F. Reichardt, Identification and characterization of a novel extracellular matrix protein nephronectin that is associated with integrin alpha8beta1 in the embryonic kidney. J. Cell Biol. 154, 447-458 (2001).
    • (2001) J. Cell Biol. , vol.154 , pp. 447-458
    • Brandenberger, R.1    Schmidt, A.2    Linton, J.3    Wang, D.4    Backus, C.5    Denda, S.6    Müller, U.7    Reichardt, L.F.8
  • 44
    • 0029972076 scopus 로고    scopus 로고
    • Myoblast fusion requires cytosolic calcium elevation but not activation of voltage-dependent calcium channels
    • B. Constantin, C. Cognard, G. Raymond, Myoblast fusion requires cytosolic calcium elevation but not activation of voltage-dependent calcium channels. Cell Calcium 19, 365-374 (1996).
    • (1996) Cell Calcium , vol.19 , pp. 365-374
    • Constantin, B.1    Cognard, C.2    Raymond, G.3
  • 46
    • 0029964141 scopus 로고    scopus 로고
    • Involvement of K(Ca) channels and stretch-activated channels in calcium infl ux, triggering membrane fusion of chick embryonic myoblasts
    • K. S. Shin, J. Y. Park, D. B. Ha, C. H. Chung, M. S. Kang, Involvement of K(Ca) channels and stretch-activated channels in calcium infl ux, triggering membrane fusion of chick embryonic myoblasts. Dev. Biol. 175, 14-23 (1996).
    • (1996) Dev. Biol. , vol.175 , pp. 14-23
    • Shin, K.S.1    Park, J.Y.2    Ha, D.B.3    Chung, C.H.4    Kang, M.S.5
  • 48
    • 0037018145 scopus 로고    scopus 로고
    • NFAT: Ubiquitous regulator of cell differentiation and adaptation
    • V. Horsley, G. K. Pavlath, NFAT: Ubiquitous regulator of cell differentiation and adaptation. J. Cell Biol. 156, 771-774 (2002).
    • (2002) J. Cell Biol. , vol.156 , pp. 771-774
    • Horsley, V.1    Pavlath, G.K.2
  • 49
    • 0035897418 scopus 로고    scopus 로고
    • Regulation of the growth of multinucleated muscle cells by an NFATC2-dependent pathway
    • V. Horsley, B. B. Friday, S. Matteson, K. M. Kegley, J. Gephart, G. K. Pavlath, Regulation of the growth of multinucleated muscle cells by an NFATC2-dependent pathway. J. Cell Biol. 153, 329-338 (2001).
    • (2001) J. Cell Biol. , vol.153 , pp. 329-338
    • Horsley, V.1    Friday, B.B.2    Matteson, S.3    Kegley, K.M.4    Gephart, J.5    Pavlath, G.K.6
  • 50
    • 0037726553 scopus 로고    scopus 로고
    • IL-4 acts as a myoblast recruitment factor during mammalian muscle growth
    • V. Horsley, K. M. Jansen, S. T. Mills, G. K. Pavlath, IL-4 acts as a myoblast recruitment factor during mammalian muscle growth. Cell 113, 483-494 (2003).
    • (2003) Cell , vol.113 , pp. 483-494
    • Horsley, V.1    Jansen, K.M.2    Mills, S.T.3    Pavlath, G.K.4
  • 52
    • 0037437175 scopus 로고    scopus 로고
    • Prostaglandin F2(alpha) stimulates growth of skeletal muscle cells via an NFATC2-dependent pathway
    • V. Horsley, G. K. Pavlath, Prostaglandin F2(alpha) stimulates growth of skeletal muscle cells via an NFATC2-dependent pathway. J. Cell Biol. 161, 111-118 (2003).
    • (2003) J. Cell Biol. , vol.161 , pp. 111-118
    • Horsley, V.1    Pavlath, G.K.2
  • 53
    • 2342640319 scopus 로고    scopus 로고
    • Cell fusion in skeletal muscle-Central role of NFATC2 in regulating muscle cell size
    • G. K. Pavlath, V. Horsley, Cell fusion in skeletal muscle-Central role of NFATC2 in regulating muscle cell size. Cell Cycle 2, 420-423 (2003).
    • (2003) Cell Cycle , vol.2 , pp. 420-423
    • Pavlath, G.K.1    Horsley, V.2
  • 57
    • 4444376712 scopus 로고    scopus 로고
    • Signaling to NF-kappaB
    • M. S. Hayden, S. Ghosh, Signaling to NF-kappaB. Genes Dev. 18, 2195-2224 (2004).
    • (2004) Genes Dev. , vol.18 , pp. 2195-2224
    • Hayden, M.S.1    Ghosh, S.2
  • 58
    • 52549133171 scopus 로고    scopus 로고
    • Nuclear factor-kappa B signaling in skeletal muscle atrophy
    • H. Li, S. Malhotra, A. Kumar, Nuclear factor-kappa B signaling in skeletal muscle atrophy. J. Mol. Med. 86, 1113-1126 (2008).
    • (2008) J. Mol. Med. , vol.86 , pp. 1113-1126
    • Li, H.1    Malhotra, S.2    Kumar, A.3
  • 60
    • 80054854922 scopus 로고    scopus 로고
    • Non-canonical NF-κB signaling activation and regulation: Principles and perspectives
    • B. Razani, A. D. Reichardt, G. Cheng, Non-canonical NF-κB signaling activation and regulation: Principles and perspectives. Immunol. Rev. 244, 44-54 (2011).
    • (2011) Immunol. Rev. , vol.244 , pp. 44-54
    • Razani, B.1    Reichardt, A.D.2    Cheng, G.3
  • 62
    • 56349164232 scopus 로고    scopus 로고
    • Nonredundant and complementary functions of TRAF2 and TRAF3 in a ubiquitination cascade that activates NIK-dependent alternative NF-kappaB signaling
    • S. Vallabhapurapu, A. Matsuzawa, W. Zhang, P. H. Tseng, J. J. Keats, H. Wang, D. A. Vignali, P. L. Bergsagel, M. Karin, Nonredundant and complementary functions of TRAF2 and TRAF3 in a ubiquitination cascade that activates NIK-dependent alternative NF-kappaB signaling. Nat. Immunol. 9, 1364-1370 (2008).
    • (2008) Nat. Immunol. , vol.9 , pp. 1364-1370
    • Vallabhapurapu, S.1    Matsuzawa, A.2    Zhang, W.3    Tseng, P.H.4    Keats, J.J.5    Wang, H.6    Vignali, D.A.7    Bergsagel, P.L.8    Karin, M.9
  • 66
    • 63249086636 scopus 로고    scopus 로고
    • Tumor necrosis factor-related weak inducer of apoptosis augments matrix metalloproteinase 9 (MMP-9) production in skeletal muscle through the activation of nuclear factor-kappaB-inducing kinase and p38 mitogen- activated protein kinase: A potential role of MMP-9 in myopathy
    • H. Li, A. Mittal, P. K. Paul, M. Kumar, D. S. Srivastava, S. C. Tyagi, A. Kumar, Tumor necrosis factor-related weak inducer of apoptosis augments matrix metalloproteinase 9 (MMP-9) production in skeletal muscle through the activation of nuclear factor-kappaB-inducing kinase and p38 mitogen- activated protein kinase: A potential role of MMP-9 in myopathy. J. Biol. Chem. 284, 4439- 4450 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 4439-4450
    • Li, H.1    Mittal, A.2    Paul, P.K.3    Kumar, M.4    Srivastava, D.S.5    Tyagi, S.C.6    Kumar, A.7
  • 68
    • 34447519304 scopus 로고    scopus 로고
    • Fibroblast growth factor inducible 14 (Fn14) is required for the expression of myogenic regulatory factors and differentiation of myoblasts into myotubes. Evidence for TWEAK-independent functions of Fn14 during myogenesis
    • C. Dogra, S. L. Hall, N. Wedhas, T. A. Linkhart, A. Kumar, Fibroblast growth factor inducible 14 (Fn14) is required for the expression of myogenic regulatory factors and differentiation of myoblasts into myotubes. Evidence for TWEAK-independent functions of Fn14 during myogenesis. J. Biol. Chem. 282, 15000-15010 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 15000-15010
    • Dogra, C.1    Hall, S.L.2    Wedhas, N.3    Linkhart, T.A.4    Kumar, A.5
  • 69
    • 33744542153 scopus 로고    scopus 로고
    • Tumor necrosis factor-like weak inducer of apoptosis inhibits skeletal myogenesis through sustained activation of nuclear factor-kappaB and degradation of MyoD protein
    • C. Dogra, H. Changotra, S. Mohan, A. Kumar, Tumor necrosis factor-like weak inducer of apoptosis inhibits skeletal myogenesis through sustained activation of nuclear factor-kappaB and degradation of MyoD protein. J. Biol. Chem. 281, 10327-10336 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 10327-10336
    • Dogra, C.1    Changotra, H.2    Mohan, S.3    Kumar, A.4
  • 70
    • 34249775509 scopus 로고    scopus 로고
    • TNF-related weak inducer of apoptosis (TWEAK) is a potent skeletal muscle- wasting cytokine
    • C. Dogra, H. Changotra, N. Wedhas, X. Qin, J. E. Wergedal, A. Kumar, TNF-related weak inducer of apoptosis (TWEAK) is a potent skeletal muscle- wasting cytokine. FASEB J. 21, 1857-1869 (2007).
    • (2007) FASEB J. , vol.21 , pp. 1857-1869
    • Dogra, C.1    Changotra, H.2    Wedhas, N.3    Qin, X.4    Wergedal, J.E.5    Kumar, A.6
  • 71
    • 77957338124 scopus 로고    scopus 로고
    • Genetic ablation of TWEAK augments regeneration and post-injury growth of skeletal muscle in mice
    • A. Mittal, S. Bhatnagar, A. Kumar, P. K. Paul, S. Kuang, A. Kumar, Genetic ablation of TWEAK augments regeneration and post-injury growth of skeletal muscle in mice. Am. J. Pathol. 177, 1732-1742 (2010).
    • (2010) Am. J. Pathol. , vol.177 , pp. 1732-1742
    • Mittal, A.1    Bhatnagar, S.2    Kumar, A.3    Paul, P.K.4    Kuang, S.5    Kumar, A.6
  • 74
    • 41549115361 scopus 로고    scopus 로고
    • Wnt/beta-catenin signaling: New (and old) players and new insights
    • H. Huang, X. He, Wnt/beta-catenin signaling: New (and old) players and new insights. Curr. Opin. Cell Biol. 20, 119-125 (2008).
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 119-125
    • Huang, H.1    He, X.2
  • 76
    • 4644352422 scopus 로고    scopus 로고
    • Insulin and wnt1 pathways cooperate to induce reserve cell activation in differentiation and myotube hypertrophy
    • A. Rochat, A. Fernandez, M. Vandromme, J. P. Molès, T. Bouschet, G. Carnac, N. J. Lamb, Insulin and wnt1 pathways cooperate to induce reserve cell activation in differentiation and myotube hypertrophy. Mol. Biol. Cell 15, 4544-4555 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4544-4555
    • Rochat, A.1    Fernandez, A.2    Vandromme, M.3    Molès, J.P.4    Bouschet, T.5    Carnac, G.6    Lamb, N.J.7
  • 77
    • 79951549830 scopus 로고    scopus 로고
    • Segregation of myoblast fusion and muscle-specific gene expression by distinct ligand-dependent inactivation of GSK-3β
    • N. A. Pansters, J. L. van der Velden, M. C. Kelders, H. Laeremans, A. M. Schols, R. C. Langen, Segregation of myoblast fusion and muscle-specific gene expression by distinct ligand-dependent inactivation of GSK-3β. Cell. Mol. Life Sci. 68, 523-535 (2011).
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 523-535
    • Pansters, N.A.1    Van Der Velden, J.L.2    Kelders, M.C.3    Laeremans, H.4    Schols, A.M.5    Langen, R.C.6
  • 78
    • 84866531872 scopus 로고    scopus 로고
    • Heparan sulfate 6-O-endosulfatases (Sulfs) coordinate the Wnt signaling pathways to regulate myoblast fusion during skeletal muscle regeneration
    • T. H. Tran, X. Shi, J. Zaia, X. Ai, Heparan sulfate 6-O-endosulfatases (Sulfs) coordinate the Wnt signaling pathways to regulate myoblast fusion during skeletal muscle regeneration. J. Biol. Chem. 287, 32651-32664 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 32651-32664
    • Tran, T.H.1    Shi, X.2    Zaia, J.3    Ai, X.4
  • 79
    • 37549039009 scopus 로고    scopus 로고
    • A temporal switch from notch to Wnt signaling in muscle stem cells is necessary for normal adult myogenesis
    • A. S. Brack, I. M. Conboy, M. J. Conboy, J. Shen, T. A. Rando, A temporal switch from notch to Wnt signaling in muscle stem cells is necessary for normal adult myogenesis. Cell Stem Cell 2, 50-59 (2008).
    • (2008) Cell Stem Cell , vol.2 , pp. 50-59
    • Brack, A.S.1    Conboy, I.M.2    Conboy, M.J.3    Shen, J.4    Rando, T.A.5
  • 80
    • 35748983572 scopus 로고    scopus 로고
    • Sulfs are regulators of growth factor signaling for satellite cell differentiation and muscle regeneration
    • A. Langsdorf, A. T. Do, M. Kusche-Gullberg, C. P. Emerson Jr., X. Ai, Sulfs are regulators of growth factor signaling for satellite cell differentiation and muscle regeneration. Dev. Biol. 311, 464-477 (2007).
    • (2007) Dev. Biol. , vol.311 , pp. 464-477
    • Langsdorf, A.1    Do, A.T.2    Kusche-Gullberg, M.3    Emerson Jr., C.P.4    Ai, X.5
  • 81
    • 0022977185 scopus 로고
    • Regulation of myogenic differentiation by type beta transforming growth factor
    • E. N. Olson, E. Sternberg, J. S. Hu, G. Spizz, C. Wilcox, Regulation of myogenic differentiation by type beta transforming growth factor. J. Cell Biol. 103, 1799-1805 (1986).
    • (1986) J. Cell Biol. , vol.103 , pp. 1799-1805
    • Olson, E.N.1    Sternberg, E.2    Hu, J.S.3    Spizz, G.4    Wilcox, C.5
  • 82
    • 84859305621 scopus 로고    scopus 로고
    • A TGFβ-Smad4-Fgf6 signaling cascade controls myogenic differentiation and myoblast fusion during tongue development
    • D. Han, H. Zhao, C. Parada, J. G. Hacia, P. Bringas, Jr, Y. Chai, A TGFβ-Smad4-Fgf6 signaling cascade controls myogenic differentiation and myoblast fusion during tongue development. Development 139, 1640-1650 (2012).
    • (2012) Development , vol.139 , pp. 1640-1650
    • Han, D.1    Zhao, H.2    Parada, C.3    Hacia, J.G.4    Bringas Jr., P.5    Chai, Y.6
  • 84
    • 77949321565 scopus 로고    scopus 로고
    • NF-kappaB functions in stromal fi broblasts to regulate early postnatal muscle development
    • J. M. Dahlman, N. Bakkar, W. He, D. C. Guttridge, NF-kappaB functions in stromal fi broblasts to regulate early postnatal muscle development. J. Biol. Chem. 285, 5479-5487 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 5479-5487
    • Dahlman, J.M.1    Bakkar, N.2    He, W.3    Guttridge, D.C.4


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