메뉴 건너뛰기




Volumn 9, Issue 11, 1998, Pages 3057-3069

Opposite effects of insulin on focal adhesion proteins in 3T3-L1 adipocytes and in cells overexpressing the insulin receptor

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CYTOSKELETON PROTEIN; INSULIN; INSULIN RECEPTOR; PAXILLIN;

EID: 0031770711     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.9.11.3057     Document Type: Article
Times cited : (21)

References (36)
  • 1
    • 0030020103 scopus 로고    scopus 로고
    • Insulin induces rapid and specific rearrangement of the cytoskeleton of rat mesangial cells in vitro
    • Berfield, A.K., Raugi, G.J., and Abrass, C.K. (1996). Insulin induces rapid and specific rearrangement of the cytoskeleton of rat mesangial cells in vitro. J. Histochem. Cytochem. 44, 91-101.
    • (1996) J. Histochem. Cytochem. , vol.44 , pp. 91-101
    • Berfield, A.K.1    Raugi, G.J.2    Abrass, C.K.3
  • 2
    • 0029896163 scopus 로고    scopus 로고
    • Regulation, substrates and functions of src
    • Brown, M.T., and Cooper, J.A. (1996). Regulation, substrates and functions of src. Biochim. Biophys. Acta 1287, 121-149.
    • (1996) Biochim. Biophys. Acta , vol.1287 , pp. 121-149
    • Brown, M.T.1    Cooper, J.A.2
  • 4
    • 0024150623 scopus 로고
    • Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton
    • Burridge, K., Fath, K., Kelly, T., Nuckolls, G., and Turner, C. (1988). Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu. Rev. Cell Biol. 4, 487-525.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 487-525
    • Burridge, K.1    Fath, K.2    Kelly, T.3    Nuckolls, G.4    Turner, C.5
  • 5
    • 0028904053 scopus 로고
    • Insulin action and the insulin signaling network
    • Cheatham, B., and Kahn, C.R. (1995). Insulin action and the insulin signaling network. Endocr. Rev. 16, 117-142.
    • (1995) Endocr. Rev. , vol.16 , pp. 117-142
    • Cheatham, B.1    Kahn, C.R.2
  • 6
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark, E.A., and Brugge, J.S. (1995). Integrins and signal transduction pathways: the road taken. Science 268, 233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 7
    • 0027976137 scopus 로고
    • Mechanisms of leukocyte motility and chemotaxis
    • Downey, G.P. (1994). Mechanisms of leukocyte motility and chemotaxis. Curr. Opin. Immunol. 6, 113-124.
    • (1994) Curr. Opin. Immunol. , vol.6 , pp. 113-124
    • Downey, G.P.1
  • 9
    • 0028340626 scopus 로고
    • Hybrid formation between endogenous mouse and transfected human tyrosine kinase-deficient (A/K1018) insulin receptors leads to decreased insulin sensitivity in 3T3-L2 adipocytes
    • Grako, K.A., McClain, D.A., and Olefsky, J.M. (1994). Hybrid formation between endogenous mouse and transfected human tyrosine kinase-deficient (A/K1018) insulin receptors leads to decreased insulin sensitivity in 3T3-L2 adipocytes. Mol. Endocrinol. 8, 682-692.
    • (1994) Mol. Endocrinol. , vol.8 , pp. 682-692
    • Grako, K.A.1    McClain, D.A.2    Olefsky, J.M.3
  • 11
    • 0028036369 scopus 로고
    • Membrane interactions with the actin cytoskeleton
    • Hitt, A.L., and Luna, E.J. (1994). Membrane interactions with the actin cytoskeleton. Curr. Opin. Cell Biol. 6, 120-130.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 120-130
    • Hitt, A.L.1    Luna, E.J.2
  • 12
    • 0028910137 scopus 로고
    • Divergent insulin and platelet-derived growth factor regulation of focal adhesion kinase (pp125FAK) tyrosine phosphorylation, and rearrangement of actin stress fibers
    • Knight, J.B., Yamauchi, K., and Pessin, J.E. (1995). Divergent insulin and platelet-derived growth factor regulation of focal adhesion kinase (pp125FAK) tyrosine phosphorylation, and rearrangement of actin stress fibers. J. Biol. Chem. 270, 10199-10203.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10199-10203
    • Knight, J.B.1    Yamauchi, K.2    Pessin, J.E.3
  • 13
    • 0029912152 scopus 로고    scopus 로고
    • Insulin and insulin-like growth factor-1 stimulate dephosphorylation of paxillin in parallel with focal adhesion kinase
    • Konstantopoulos, N., and Clark, S. (1996). Insulin and insulin-like growth factor-1 stimulate dephosphorylation of paxillin in parallel with focal adhesion kinase. Biochem. J. 314, 387-390.
    • (1996) Biochem. J. , vol.314 , pp. 387-390
    • Konstantopoulos, N.1    Clark, S.2
  • 14
    • 0019756309 scopus 로고
    • Insulin receptor synthesis and turnover in differentiating 3T3-L1 preadipocytes
    • Lane, M.D., Reed, R.C., and Clements, P.R. (1981). Insulin receptor synthesis and turnover in differentiating 3T3-L1 preadipocytes. Prog. Clin. Biol. Res. 66, 523-542.
    • (1981) Prog. Clin. Biol. Res. , vol.66 , pp. 523-542
    • Lane, M.D.1    Reed, R.C.2    Clements, P.R.3
  • 15
    • 0030995946 scopus 로고    scopus 로고
    • The 60-kDa phosphotyrosine protein in insulin-treated adipocytes is a new member of the insulin receptor substrate family
    • Lavan, B.E., Lane, W.S., and Lienhard, G.E. (1997). The 60-kDa phosphotyrosine protein in insulin-treated adipocytes is a new member of the insulin receptor substrate family. J. Biol. Chem. 272, 11439-11443.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11439-11443
    • Lavan, B.E.1    Lane, W.S.2    Lienhard, G.E.3
  • 16
    • 0029973135 scopus 로고    scopus 로고
    • Activated phosphatidylinositol 3-kinase is sufficient to mediate actin rearrangement and GLUT4 translocation in 3T3-L1 adipocytes
    • Martin, S.S., Haruta, T., Morris, A.J., Klippel, A., Williams, L.T., and Olefsky, J.M. (1996). Activated phosphatidylinositol 3-kinase is sufficient to mediate actin rearrangement and GLUT4 translocation in 3T3-L1 adipocytes. J. Biol. Chem. 271, 17605-17608.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17605-17608
    • Martin, S.S.1    Haruta, T.2    Morris, A.J.3    Klippel, A.4    Williams, L.T.5    Olefsky, J.M.6
  • 17
    • 33745345159 scopus 로고    scopus 로고
    • Putting the actin cytoskeleton into perspective: Pathophysiology of ischemic alterations
    • Molitoris, B.A. (1997). Putting the actin cytoskeleton into perspective: pathophysiology of ischemic alterations. Am. J. Physiol. 272, F430-F433.
    • (1997) Am. J. Physiol. , vol.272
    • Molitoris, B.A.1
  • 18
    • 0028837170 scopus 로고
    • Activation of the small GTP-binding protein rho and rac by growth factor receptors
    • Nobes, C.D., Hawkins, P., Stephens, L., and Hall, A. (1995). Activation of the small GTP-binding protein rho and rac by growth factor receptors. J. Cell Sci. 108, 225-233.
    • (1995) J. Cell Sci. , vol.108 , pp. 225-233
    • Nobes, C.D.1    Hawkins, P.2    Stephens, L.3    Hall, A.4
  • 19
    • 0029666080 scopus 로고    scopus 로고
    • FAK in the focal adhesion
    • FAK in the focal adhesion. Int. Rev. Cytol. 167, 161-183.
    • (1996) Int. Rev. Cytol. , vol.167 , pp. 161-183
    • Otey, C.A.1
  • 20
    • 0029965695 scopus 로고    scopus 로고
    • Integrin-mediated signaling: Regulation by protein tyrosine kinases and small GTP-binding proteins
    • Parsons, J.T. (1996). Integrin-mediated signaling: regulation by protein tyrosine kinases and small GTP-binding proteins. Curr. Opin. Cell Biol. 8, 146-152.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 146-152
    • Parsons, J.T.1
  • 21
    • 0028837993 scopus 로고
    • Insulin stimulates the tyrosine dephosphorylation of pp125 Focal adhesion kinase
    • Pillay, T.S., Sasaoka, T., and Olefsky, J.M. (1995). Insulin stimulates the tyrosine dephosphorylation of pp125 Focal adhesion kinase. J. Biol. Chem. 270, 991-994.
    • (1995) J. Biol. Chem. , vol.270 , pp. 991-994
    • Pillay, T.S.1    Sasaoka, T.2    Olefsky, J.M.3
  • 22
    • 0027466903 scopus 로고
    • Insulin-induced phosphorylation of the 46- And 52-KDa Shc proteins
    • Pronk, G.J., McGlade, J., Pelicci, G., Pawson, T., and Bos, J.L. (1993). Insulin-induced phosphorylation of the 46-and 52-KDa Shc proteins. J. Biol. Chem. 268, 5748-5753.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5748-5753
    • Pronk, G.J.1    McGlade, J.2    Pelicci, G.3    Pawson, T.4    Bos, J.L.5
  • 23
    • 0028049088 scopus 로고
    • Platelet-derived growth factor modulation of focal adhesion kinase (P125FAK) and paxillin tyrosine phosphorylation in Swiss 3T3 cells
    • Rankin, S., and Rozengurt, E. (1994). Platelet-derived growth factor modulation of focal adhesion kinase (P125FAK) and paxillin tyrosine phosphorylation in Swiss 3T3 cells. J. Biol. Chem. 269, 704-710.
    • (1994) J. Biol. Chem. , vol.269 , pp. 704-710
    • Rankin, S.1    Rozengurt, E.2
  • 24
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A.J., and Hall, A. (1992). The small GTP-binding protein rho regulates assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70, 389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 25
    • 0028350859 scopus 로고
    • Autophosphorylation of the focal adhesion kinase pp 125FAK, directs SH2-dependent binding of pp60src
    • Schaller, M.D., Hildebrand, J.D., Shannon, J.D., Fox, J.W., Vines, R.R., and Parsons, J.T. (1994). Autophosphorylation of the focal adhesion kinase pp 125FAK, directs SH2-dependent binding of pp60src. Mol. Cell. Biol. 14, 1680-1688.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1680-1688
    • Schaller, M.D.1    Hildebrand, J.D.2    Shannon, J.D.3    Fox, J.W.4    Vines, R.R.5    Parsons, J.T.6
  • 26
    • 0030926774 scopus 로고    scopus 로고
    • Focal adhesion kinase overexpression enhances Ras-dependent intregin signaling to ERK2/ mitogen-activated protein kinase through interactions with and activation of c-Src
    • Schlaepfer, D.D., and Hunter, T. (1997). Focal adhesion kinase overexpression enhances Ras-dependent intregin signaling to ERK2/ mitogen-activated protein kinase through interactions with and activation of c-Src. J. Biol. Chem. 272, 13189-13195.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13189-13195
    • Schlaepfer, D.D.1    Hunter, T.2
  • 27
    • 9444267146 scopus 로고    scopus 로고
    • Csk enhances insulin-stimulated dephosphorylation of focal adhesion proteins
    • Tobe, K., et al. (1996). Csk enhances insulin-stimulated dephosphorylation of focal adhesion proteins. Mol. Cell. Biol. 16, 4765-4772.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4765-4772
    • Tobe, K.1
  • 28
    • 0027489573 scopus 로고
    • Cytoskeleton dynamics during neurotransmitter release
    • Trifaro, J.M., and Vitale, M.L. (1993). Cytoskeleton dynamics during neurotransmitter release. Trends Neurosci. 16, 466-472.
    • (1993) Trends Neurosci. , vol.16 , pp. 466-472
    • Trifaro, J.M.1    Vitale, M.L.2
  • 29
    • 0028126854 scopus 로고
    • Disassembly of the actin network inhibits insulin-dependent stimulation of glucose transport and prevents recruitment of glucose transporters to the plasma membrane
    • Tsakiridis, T., Vranic, M., and Klip, A. (1994). Disassembly of the actin network inhibits insulin-dependent stimulation of glucose transport and prevents recruitment of glucose transporters to the plasma membrane. J. Biol. Chem. 269, 29934-29942.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29934-29942
    • Tsakiridis, T.1    Vranic, M.2    Klip, A.3
  • 30
    • 0028840159 scopus 로고
    • Chromaffin cell cortical actin network dynamics control the size of the release-ready vesicle pool and the initial rate of exocytosis
    • Vitale, M.L., Seward, E.P., and Trifaro, J.M. (1995). Chromaffin cell cortical actin network dynamics control the size of the release-ready vesicle pool and the initial rate of exocytosis. Neuron 14, 353-363.
    • (1995) Neuron , vol.14 , pp. 353-363
    • Vitale, M.L.1    Seward, E.P.2    Trifaro, J.M.3
  • 31
    • 0028918978 scopus 로고
    • Cellubrevin is a resident protein of insulin-sensitive GLUT4 glucose transporter vesicles in 3T3-L1 adipocytes
    • Volchuk, A., Sargeant, R., Sumitani, S., Liu, Z., He, L., and Klip, A. (1995). Cellubrevin is a resident protein of insulin-sensitive GLUT4 glucose transporter vesicles in 3T3-L1 adipocytes. J. Biol. Chem. 270, 8233-8240.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8233-8240
    • Volchuk, A.1    Sargeant, R.2    Sumitani, S.3    Liu, Z.4    He, L.5    Klip, A.6
  • 32
    • 0030780582 scopus 로고    scopus 로고
    • The small guanosine triphosphate-binding protein Rab4 is involved in insulin-induced GLUT4 translocation and actin filament rearrangement in 3T3-L1 cells
    • Vollenweider, P., Martin, S.S., Haruta, T., Morris, A.J., Nelson, J.G., Cormont, N., Le Marchand-Brustel, Y., Rose, D.W., and Olefsky, J.M. (1997). The small guanosine triphosphate-binding protein Rab4 is involved in insulin-induced GLUT4 translocation and actin filament rearrangement in 3T3-L1 cells. Endocrinology 138, 4941-4949.
    • (1997) Endocrinology , vol.138 , pp. 4941-4949
    • Vollenweider, P.1    Martin, S.S.2    Haruta, T.3    Morris, A.J.4    Nelson, J.G.5    Cormont, N.6    Le Marchand-Brustel, Y.7    Rose, D.W.8    Olefsky, J.M.9
  • 33
    • 0032080114 scopus 로고    scopus 로고
    • Actin filaments participate in the relocalization of phosphatidylinositol 3-kinase to glucose transporter-containing compartments and in the stimulation of glucose uptake in 3T3-L1 adipocytes
    • Wang, Q., Bilan, P.J., Tsakiridis, T., Hinek, A., and Klip, A. (1998). Actin filaments participate in the relocalization of phosphatidylinositol 3-kinase to glucose transporter-containing compartments and in the stimulation of glucose uptake in 3T3-L1 adipocytes. Biochem. J. 331, 917-928.
    • (1998) Biochem. J. , vol.331 , pp. 917-928
    • Wang, Q.1    Bilan, P.J.2    Tsakiridis, T.3    Hinek, A.4    Klip, A.5
  • 34
    • 0030748457 scopus 로고    scopus 로고
    • The insulin signaling system and the IRS proteins
    • White, M.F. (1997). The insulin signaling system and the IRS proteins. Diabetologia 40, S2-S17.
    • (1997) Diabetologia , vol.40
    • White, M.F.1
  • 35
    • 0028085078 scopus 로고
    • The insulin signaling system
    • White, M.F., and Kahn, C.R. (1994). The insulin signaling system. J. Biol. Chem. 269, 1-4.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1-4
    • White, M.F.1    Kahn, C.R.2
  • 36
    • 0028036724 scopus 로고
    • Insulin receptor substrate-1 (IRS) and Shc compete for a limited pool of Grb2 in mediating insulin downstream signaling
    • Yamauchi, K., and Pessin, J.E. (1994). Insulin receptor substrate-1 (IRS) and Shc compete for a limited pool of Grb2 in mediating insulin downstream signaling. J. Biol. Chem. 269, 31107-31114.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31107-31114
    • Yamauchi, K.1    Pessin, J.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.