메뉴 건너뛰기




Volumn 89, Issue 5, 2010, Pages 351-364

Ponsin interacts with Nck adapter proteins: implications for a role in cytoskeletal remodelling during differentiation of skeletal muscle cells

Author keywords

Mitogen activated protein kinase (MAPK); Nck; Ponsin; Protein phosphorylation; Skeletal muscle cell differentiation

Indexed keywords

ADAPTOR PROTEIN; NCK PROTEIN; NCK1 PROTEIN; NCK2 PROTEIN; PONSIN; PROLINE; UNCLASSIFIED DRUG;

EID: 77049095097     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejcb.2009.10.019     Document Type: Article
Times cited : (5)

References (48)
  • 2
    • 43849085150 scopus 로고    scopus 로고
    • Exercise training increases components of the c-Cbl-associated protein/c-Cbl signaling cascade in muscle of obese Zucker rats
    • Bernard J.R., Saito M., Liao Y.H., Yaspelkis III B.B., and Ivy J.L. Exercise training increases components of the c-Cbl-associated protein/c-Cbl signaling cascade in muscle of obese Zucker rats. Metabolism 57 (2008) 858-866
    • (2008) Metabolism , vol.57 , pp. 858-866
    • Bernard, J.R.1    Saito, M.2    Liao, Y.H.3    Yaspelkis III, B.B.4    Ivy, J.L.5
  • 3
    • 0038383014 scopus 로고    scopus 로고
    • The murine Nck SH2/SH3 adaptors are important for the development of mesoderm-derived embryonic structures and for regulating the cellular actin network
    • Bladt F., Aippersbach E., Gelkop S., Strasser G.A., Nash P., Tafuri A., Gertler F.B., and Pawson T. The murine Nck SH2/SH3 adaptors are important for the development of mesoderm-derived embryonic structures and for regulating the cellular actin network. Mol. Cell. Biol. 23 (2003) 4586-4597
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4586-4597
    • Bladt, F.1    Aippersbach, E.2    Gelkop, S.3    Strasser, G.A.4    Nash, P.5    Tafuri, A.6    Gertler, F.B.7    Pawson, T.8
  • 4
    • 0036015163 scopus 로고    scopus 로고
    • The Nck family of adapter proteins: regulators of actin cytoskeleton
    • Buday L., Wunderlich L., and Tamas P. The Nck family of adapter proteins: regulators of actin cytoskeleton. Cell Signal. 14 (2002) 723-731
    • (2002) Cell Signal. , vol.14 , pp. 723-731
    • Buday, L.1    Wunderlich, L.2    Tamas, P.3
  • 7
    • 0242468210 scopus 로고    scopus 로고
    • Duchenne's muscular dystrophy: animal models used to investigate pathogenesis and develop therapeutic strategies
    • Collins C.A., and Morgan J.E. Duchenne's muscular dystrophy: animal models used to investigate pathogenesis and develop therapeutic strategies. Int. J. Exp. Pathol. 84 (2003) 165-172
    • (2003) Int. J. Exp. Pathol. , vol.84 , pp. 165-172
    • Collins, C.A.1    Morgan, J.E.2
  • 8
    • 0036549872 scopus 로고    scopus 로고
    • Cardiac expression and subcellular localization of the p38 mitogen-activated protein kinase member, stress-activated protein kinase-3 (SAPK3)
    • Court N.W., dos Remedios C.G., Cordell J., and Bogoyevitch M.A. Cardiac expression and subcellular localization of the p38 mitogen-activated protein kinase member, stress-activated protein kinase-3 (SAPK3). J. Mol. Cell. Cardiol. 34 (2002) 413-426
    • (2002) J. Mol. Cell. Cardiol. , vol.34 , pp. 413-426
    • Court, N.W.1    dos Remedios, C.G.2    Cordell, J.3    Bogoyevitch, M.A.4
  • 9
    • 0035855819 scopus 로고    scopus 로고
    • The SH2/SH3 adaptor Grb4 transduces B-ephrin reverse signals
    • Cowan C.A., and Henkemeyer M. The SH2/SH3 adaptor Grb4 transduces B-ephrin reverse signals. Nature 413 (2001) 174-179
    • (2001) Nature , vol.413 , pp. 174-179
    • Cowan, C.A.1    Henkemeyer, M.2
  • 10
    • 0028988138 scopus 로고
    • SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1
    • Cuenda A., Rouse J., Doza Y.N., Meier R., Cohen P., Gallagher T.F., Young P.R., and Lee J.C. SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1. FEBS Lett. 364 (1995) 229-233
    • (1995) FEBS Lett. , vol.364 , pp. 229-233
    • Cuenda, A.1    Rouse, J.2    Doza, Y.N.3    Meier, R.4    Cohen, P.5    Gallagher, T.F.6    Young, P.R.7    Lee, J.C.8
  • 11
    • 0027165150 scopus 로고
    • The mitogen-activated protein kinase signal transduction pathway
    • Davis R.J. The mitogen-activated protein kinase signal transduction pathway. J. Biol. Chem. 268 (1993) 14553-14556
    • (1993) J. Biol. Chem. , vol.268 , pp. 14553-14556
    • Davis, R.J.1
  • 12
    • 0034769309 scopus 로고    scopus 로고
    • Extracellular signal regulated kinase 5 (ERK5) is required for the differentiation of muscle cells
    • Dinev D., Jordan B.W., Neufeld B., Lee J.D., Lindemann D., Rapp U.R., and Ludwig S. Extracellular signal regulated kinase 5 (ERK5) is required for the differentiation of muscle cells. EMBO Rep. 2 (2001) 829-834
    • (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
  • 14
    • 4043152847 scopus 로고    scopus 로고
    • Decreased interactions of mutant muscle LIM protein (MLP) with N-RAP and alpha-actinin and their implication for hypertrophic cardiomyopathy
    • Gehmlich K., Geier C., Osterziel K.J., Van der Ven P.F., and Fürst D.O. Decreased interactions of mutant muscle LIM protein (MLP) with N-RAP and alpha-actinin and their implication for hypertrophic cardiomyopathy. Cell Tissue Res. 317 (2004) 129-136
    • (2004) Cell Tissue Res. , vol.317 , pp. 129-136
    • Gehmlich, K.1    Geier, C.2    Osterziel, K.J.3    Van der Ven, P.F.4    Fürst, D.O.5
  • 18
    • 34548243624 scopus 로고    scopus 로고
    • Nckbeta adapter controls neuritogenesis by maintaining the cellular paxillin level
    • Guan S., Chen M., Woodley D., and Li W. Nckbeta adapter controls neuritogenesis by maintaining the cellular paxillin level. Mol. Cell. Biol. 27 (2007) 6001-6011
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 6001-6011
    • Guan, S.1    Chen, M.2    Woodley, D.3    Li, W.4
  • 19
    • 40549139084 scopus 로고    scopus 로고
    • Specificity determinants of a novel Nck interaction with the juxtamembrane domain of the epidermal growth factor receptor
    • Hake M.J., Choowongkomon K., Kostenko O., Carlin C.R., and Sonnichsen F.D. Specificity determinants of a novel Nck interaction with the juxtamembrane domain of the epidermal growth factor receptor. Biochemistry 47 (2008) 3096-3108
    • (2008) Biochemistry , vol.47 , pp. 3096-3108
    • Hake, M.J.1    Choowongkomon, K.2    Kostenko, O.3    Carlin, C.R.4    Sonnichsen, F.D.5
  • 21
    • 0035979221 scopus 로고    scopus 로고
    • The sorbin homology domain: a motif for the targeting of proteins to lipid rafts
    • Kimura A., Baumann C.A., Chiang S.H., and Saltiel A.R. The sorbin homology domain: a motif for the targeting of proteins to lipid rafts. Proc. Natl. Acad. Sci. USA 98 (2001) 9098-9103
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9098-9103
    • Kimura, A.1    Baumann, C.A.2    Chiang, S.H.3    Saltiel, A.R.4
  • 22
    • 0036257343 scopus 로고    scopus 로고
    • Vinexin, CAP/ponsin, ArgBP2: a novel adaptor protein family regulating cytoskeletal organization and signal transduction
    • Kioka N., Ueda K., and Amachi T. Vinexin, CAP/ponsin, ArgBP2: a novel adaptor protein family regulating cytoskeletal organization and signal transduction. Cell Struct. Funct. 27 (2002) 1-7
    • (2002) Cell Struct. Funct. , vol.27 , pp. 1-7
    • Kioka, N.1    Ueda, K.2    Amachi, T.3
  • 24
    • 54149118929 scopus 로고    scopus 로고
    • Reggies/flotillins regulate cytoskeletal remodeling during neuronal differentiation via CAP/ponsin and Rho GTPases
    • Langhorst M.F., Jaeger F.A., Mueller S., Sven H.L., Luxenhofer G., and Stuermer C.A. Reggies/flotillins regulate cytoskeletal remodeling during neuronal differentiation via CAP/ponsin and Rho GTPases. Eur. J. Cell Biol. 87 (2008) 921-931
    • (2008) Eur. J. Cell Biol. , vol.87 , pp. 921-931
    • Langhorst, M.F.1    Jaeger, F.A.2    Mueller, S.3    Sven, H.L.4    Luxenhofer, G.5    Stuermer, C.A.6
  • 25
    • 36749061251 scopus 로고    scopus 로고
    • Skeletal muscle satellite cells and adult myogenesis
    • Le G.F., and Rudnicki M.A. Skeletal muscle satellite cells and adult myogenesis. Curr. Opin. Cell Biol. 19 (2007) 628-633
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 628-633
    • Le, G.F.1    Rudnicki, M.A.2
  • 27
  • 29
    • 0035872815 scopus 로고    scopus 로고
    • Cloning, mapping, and characterization of the human sorbin and SH3 domain containing 1 (SORBS1) gene: a protein associated with c-Abl during insulin signaling in the hepatoma cell line Hep3B
    • Lin W.H., Huang C.J., Liu M.W., Chang H.M., Chen Y.J., Tai T.Y., and Chuang L.M. Cloning, mapping, and characterization of the human sorbin and SH3 domain containing 1 (SORBS1) gene: a protein associated with c-Abl during insulin signaling in the hepatoma cell line Hep3B. Genomics 74 (2001) 12-20
    • (2001) Genomics , vol.74 , pp. 12-20
    • Lin, W.H.1    Huang, C.J.2    Liu, M.W.3    Chang, H.M.4    Chen, Y.J.5    Tai, T.Y.6    Chuang, L.M.7
  • 30
    • 33745016248 scopus 로고    scopus 로고
    • Structural insight into the binding diversity between the human Nck2 SH3 domains and proline-rich proteins
    • Liu J., Li M., Ran X., Fan J.S., and Song J. Structural insight into the binding diversity between the human Nck2 SH3 domains and proline-rich proteins. Biochemistry 45 (2006) 7171-7184
    • (2006) Biochemistry , vol.45 , pp. 7171-7184
    • Liu, J.1    Li, M.2    Ran, X.3    Fan, J.S.4    Song, J.5
  • 31
    • 0037138411 scopus 로고    scopus 로고
    • WW and SH3 domains, two different scaffolds to recognize proline-rich ligands
    • Macias M.J., Wiesner S., and Sudol M. WW and SH3 domains, two different scaffolds to recognize proline-rich ligands. FEBS Lett. 513 (2002) 30-37
    • (2002) FEBS Lett. , vol.513 , pp. 30-37
    • Macias, M.J.1    Wiesner, S.2    Sudol, M.3
  • 32
    • 13444304286 scopus 로고    scopus 로고
    • A novel isoform of Cbl-associated protein that binds protein kinase A
    • Matson S.A., Pare G.C., and Kapiloff M.S. A novel isoform of Cbl-associated protein that binds protein kinase A. Biochim. Biophys. Acta 1727 (2005) 145-149
    • (2005) Biochim. Biophys. Acta , vol.1727 , pp. 145-149
    • Matson, S.A.1    Pare, G.C.2    Kapiloff, M.S.3
  • 33
    • 0017696571 scopus 로고
    • High resolution two-dimensional electrophoresis of basic as well as acidic proteins
    • O'Farrell P.Z., Goodman H.M., and O'Farrell P.H. High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell 12 (1977) 1133-1141
    • (1977) Cell , vol.12 , pp. 1133-1141
    • O'Farrell, P.Z.1    Goodman, H.M.2    O'Farrell, P.H.3
  • 34
    • 0029836627 scopus 로고    scopus 로고
    • The structure of the sarcomeric M band: localization of defined domains of myomesin, M-protein, and the 250-kD carboxy-terminal region of titin by immunoelectron microscopy
    • Obermann W.M., Gautel M., Steiner F., Van der Ven P.F., Weber K., and Fürst D.O. The structure of the sarcomeric M band: localization of defined domains of myomesin, M-protein, and the 250-kD carboxy-terminal region of titin by immunoelectron microscopy. J. Cell Biol. 134 (1996) 1441-1453
    • (1996) J. Cell Biol. , vol.134 , pp. 1441-1453
    • Obermann, W.M.1    Gautel, M.2    Steiner, F.3    Van der Ven, P.F.4    Weber, K.5    Fürst, D.O.6
  • 35
    • 0031034775 scopus 로고    scopus 로고
    • Molecular structure of the sarcomeric M band: mapping of titin and myosin binding domains in myomesin and the identification of a potential regulatory phosphorylation site in myomesin
    • Obermann W.M., Gautel M., Weber K., and Furst D.O. Molecular structure of the sarcomeric M band: mapping of titin and myosin binding domains in myomesin and the identification of a potential regulatory phosphorylation site in myomesin. EMBO J. 16 (1997) 211-220
    • (1997) EMBO J. , vol.16 , pp. 211-220
    • Obermann, W.M.1    Gautel, M.2    Weber, K.3    Furst, D.O.4
  • 36
    • 0010935732 scopus 로고
    • A vinculin-containing cortical lattice in skeletal muscle: transverse lattice elements ("costameres") mark sites of attachment between myofibrils and sarcolemma
    • Pardo J.V., Siliciano J.D., and Craig S.W. A vinculin-containing cortical lattice in skeletal muscle: transverse lattice elements ("costameres") mark sites of attachment between myofibrils and sarcolemma. Proc. Natl. Acad. Sci. USA 80 (1983) 1008-1012
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 1008-1012
    • Pardo, J.V.1    Siliciano, J.D.2    Craig, S.W.3
  • 38
    • 64049089237 scopus 로고    scopus 로고
    • Abundant expression of ponsin, a focal adhesion protein, in lens and downregulation of its expression by impaired cytoskeletal signaling
    • Rao P.V., and Maddala R. Abundant expression of ponsin, a focal adhesion protein, in lens and downregulation of its expression by impaired cytoskeletal signaling. Invest. Ophthalmol. Vis. Sci. 50 (2009) 1769-1777
    • (2009) Invest. Ophthalmol. Vis. Sci. , vol.50 , pp. 1769-1777
    • Rao, P.V.1    Maddala, R.2
  • 39
    • 0032512821 scopus 로고    scopus 로고
    • A role for CAP, a novel, multifunctional Src homology 3 domain-containing protein in formation of actin stress fibers and focal adhesions
    • Ribon V., Herrera R., Kay B.K., and Saltiel A.R. A role for CAP, a novel, multifunctional Src homology 3 domain-containing protein in formation of actin stress fibers and focal adhesions. J. Biol. Chem. 273 (1998) 4073-4080
    • (1998) J. Biol. Chem. , vol.273 , pp. 4073-4080
    • Ribon, V.1    Herrera, R.2    Kay, B.K.3    Saltiel, A.R.4
  • 40
    • 0031594145 scopus 로고    scopus 로고
    • A novel, multifuntional c-Cbl binding protein in insulin receptor signaling in 3T3-L1 adipocytes
    • Ribon V., Printen J.A., Hoffman N.G., Kay B.K., and Saltiel A.R. A novel, multifuntional c-Cbl binding protein in insulin receptor signaling in 3T3-L1 adipocytes. Mol. Cell. Biol. 18 (1998) 872-879
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 872-879
    • Ribon, V.1    Printen, J.A.2    Hoffman, N.G.3    Kay, B.K.4    Saltiel, A.R.5
  • 41
    • 1242265771 scopus 로고    scopus 로고
    • Actin polymerization: riding the wave
    • Smith L.G., and Li R. Actin polymerization: riding the wave. Curr. Biol. 14 (2004) R109-R111
    • (2004) Curr. Biol. , vol.14
    • Smith, L.G.1    Li, R.2
  • 42
    • 0038054248 scopus 로고    scopus 로고
    • ERK6 is expressed in a developmentally regulated manner in rodent skeletal muscle
    • Tortorella L.L., Lin C.B., and Pilch P.F. ERK6 is expressed in a developmentally regulated manner in rodent skeletal muscle. Biochem. Biophys. Res. Commun. 306 (2003) 163-168
    • (2003) Biochem. Biophys. Res. Commun. , vol.306 , pp. 163-168
    • Tortorella, L.L.1    Lin, C.B.2    Pilch, P.F.3
  • 43
    • 58149519189 scopus 로고    scopus 로고
    • CAP (Cbl associated protein) regulates receptor-mediated endocytosis
    • Tosoni D., and Cestra G. CAP (Cbl associated protein) regulates receptor-mediated endocytosis. FEBS Lett. 583 (2009) 293-300
    • (2009) FEBS Lett. , vol.583 , pp. 293-300
    • Tosoni, D.1    Cestra, G.2
  • 44
    • 0031772910 scopus 로고    scopus 로고
    • Nck-2, a novel Src homology2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathways
    • Tu Y., Li F., and Wu C. Nck-2, a novel Src homology2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathways. Mol. Biol. Cell 9 (1998) 3367-3382
    • (1998) Mol. Biol. Cell , vol.9 , pp. 3367-3382
    • Tu, Y.1    Li, F.2    Wu, C.3
  • 46
    • 61949147263 scopus 로고    scopus 로고
    • The rate of N-WASP exchange limits the extent of ARP2/3-complex-dependent actin-based motility
    • Weisswange I., Newsome T.P., Schleich S., and Way M. The rate of N-WASP exchange limits the extent of ARP2/3-complex-dependent actin-based motility. Nature 458 (2009) 87-91
    • (2009) Nature , vol.458 , pp. 87-91
    • Weisswange, I.1    Newsome, T.P.2    Schleich, S.3    Way, M.4
  • 47
    • 33751103910 scopus 로고    scopus 로고
    • CAP interacts with cytoskeletal proteins and regulates adhesion-mediated ERK activation and motility
    • Zhang M., Liu J., Cheng A., Deyoung S.M., Chen X., Dold L.H., and Saltiel A.R. CAP interacts with cytoskeletal proteins and regulates adhesion-mediated ERK activation and motility. EMBO J. 25 (2006) 5284-5293
    • (2006) EMBO J. , vol.25 , pp. 5284-5293
    • Zhang, M.1    Liu, J.2    Cheng, A.3    Deyoung, S.M.4    Chen, X.5    Dold, L.H.6    Saltiel, A.R.7
  • 48
    • 37049014913 scopus 로고    scopus 로고
    • Identification of CAP as a costameric protein that interacts with filamin C
    • Zhang M., Liu J., Cheng A., Deyoung S.M., and Saltiel A.R. Identification of CAP as a costameric protein that interacts with filamin C. Mol. Biol. Cell 18 (2007) 4731-4740
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4731-4740
    • Zhang, M.1    Liu, J.2    Cheng, A.3    Deyoung, S.M.4    Saltiel, A.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.