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Volumn 25, Issue 8, 2000, Pages 388-391

Signaling networks linking integrins and Rho family GTPases

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATASE; INTEGRIN; RHO FACTOR;

EID: 0034256024     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(00)01605-4     Document Type: Review
Times cited : (270)

References (50)
  • 1
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall A. Rho GTPases and the actin cytoskeleton. Science. 279:1998;509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 2
    • 0029791373 scopus 로고    scopus 로고
    • The small GTPase Rho: Cellular functions and signal transduction
    • Narumiya S. The small GTPase Rho: cellular functions and signal transduction. J. Biochem. 120:1996;215-228.
    • (1996) J. Biochem. , vol.120 , pp. 215-228
    • Narumiya, S.1
  • 3
    • 0033064738 scopus 로고    scopus 로고
    • Integrin-mediated signal transduction pathways
    • Cary L.A.et al. Integrin-mediated signal transduction pathways. Histol. Histopath. 14:1999;1001-1009.
    • (1999) Histol. Histopath. , vol.14 , pp. 1001-1009
    • Cary, L.A.1
  • 4
  • 6
    • 0031844821 scopus 로고    scopus 로고
    • Activation of Rac and Cdc42 by integrins mediates cell spreading
    • Price L.S.et al. Activation of Rac and Cdc42 by integrins mediates cell spreading. Mol. Biol. Cell. 9:1998;1863-1871.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1863-1871
    • Price, L.S.1
  • 7
    • 0034595381 scopus 로고    scopus 로고
    • Adhesion to the extracellular matrix regulates the coupling of the small GTPase Rac to it effector PAK
    • DelPozo M.A.et al. Adhesion to the extracellular matrix regulates the coupling of the small GTPase Rac to it effector PAK. EMBO J. 19:2000;2008-2014.
    • (2000) EMBO J. , vol.19 , pp. 2008-2014
    • DelPozo, M.A.1
  • 8
    • 0033081753 scopus 로고    scopus 로고
    • Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton
    • Ren X.D.et al. Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton. EMBO J. 18:1999;578-585.
    • (1999) EMBO J. , vol.18 , pp. 578-585
    • Ren, X.D.1
  • 9
    • 0026603414 scopus 로고
    • Protein kinase C involvement in focal adhesion formation
    • Woods A., Couchman J.R. Protein kinase C involvement in focal adhesion formation. J. Cell Sci. 101:1992;277-290.
    • (1992) J. Cell Sci. , vol.101 , pp. 277-290
    • Woods, A.1    Couchman, J.R.2
  • 10
    • 0033017955 scopus 로고    scopus 로고
    • Syndecan-4 signals cooperatively with integrins in a Rho-dependent manner in the assembly of focal adhesions and actin stress fibers
    • Saoncella S.et al. Syndecan-4 signals cooperatively with integrins in a Rho-dependent manner in the assembly of focal adhesions and actin stress fibers. Proc. Natl. Acad. Sci. U. S. A. 96:1999;2805-2810.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 2805-2810
    • Saoncella, S.1
  • 11
    • 0032925217 scopus 로고    scopus 로고
    • Fibronectin regulates assembly of actin filaments and focal contacts in cultured cells via the heparin-binding site in repeat III13
    • Bloom L.et al. Fibronectin regulates assembly of actin filaments and focal contacts in cultured cells via the heparin-binding site in repeat III13. Mol. Biol. Cell. 10:1999;1521-1536.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1521-1536
    • Bloom, L.1
  • 12
    • 0034050724 scopus 로고    scopus 로고
    • Syndecan-4 deficiency impairs focal adhesion formation only under restricted conditions
    • Ishiguro K.et al. Syndecan-4 deficiency impairs focal adhesion formation only under restricted conditions. J. Biol. Chem. 275:2000;5249-5252.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5249-5252
    • Ishiguro, K.1
  • 13
    • 0032572557 scopus 로고    scopus 로고
    • Integrin-mediated signals regulated by members of the rho family of GTPases
    • Clark E.A.et al. Integrin-mediated signals regulated by members of the rho family of GTPases. J. Cell Biol. 142:1998;573-586.
    • (1998) J. Cell Biol. , vol.142 , pp. 573-586
    • Clark, E.A.1
  • 14
    • 0033605651 scopus 로고    scopus 로고
    • Activation of the Cdc42-associated tyrosine kinase-2 (ACK-2) by cell adhesion via integrin beta1
    • Yang W.et al. Activation of the Cdc42-associated tyrosine kinase-2 (ACK-2) by cell adhesion via integrin beta1. J. Biol. Chem. 274:1999;8524-8530.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8524-8530
    • Yang, W.1
  • 15
    • 0032416722 scopus 로고    scopus 로고
    • The adaptor protein Crk connects multiple cellular stimuli to the JNK signaling pathway
    • Dolfi F.et al. The adaptor protein Crk connects multiple cellular stimuli to the JNK signaling pathway. Proc. Natl. Acad. Sci. U. S. A. 95:1998;15394-15399.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 15394-15399
    • Dolfi, F.1
  • 16
    • 0029828456 scopus 로고    scopus 로고
    • Involvement of the small GTPase rho in integrin-mediated activation of mitogen-activated protein kinase
    • Renshaw M.W.et al. Involvement of the small GTPase rho in integrin-mediated activation of mitogen-activated protein kinase. J. Biol. Chem. 271:1996;21691-21694.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21691-21694
    • Renshaw, M.W.1
  • 17
    • 0030963016 scopus 로고    scopus 로고
    • Requirement for Rho in integrin signalling
    • Barry S.T.et al. Requirement for Rho in integrin signalling. Cell Adhes. Commun. 4:1997;387-398.
    • (1997) Cell Adhes. Commun. , vol.4 , pp. 387-398
    • Barry, S.T.1
  • 18
    • 0028036684 scopus 로고
    • The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells
    • Chong L.D.et al. The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells. Cell. 79:1994;507-513.
    • (1994) Cell , vol.79 , pp. 507-513
    • Chong, L.D.1
  • 19
    • 0031033292 scopus 로고    scopus 로고
    • Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product
    • Crespo P.et al. Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product. Nature. 385:1997;169-172.
    • (1997) Nature , vol.385 , pp. 169-172
    • Crespo, P.1
  • 20
    • 0032898437 scopus 로고    scopus 로고
    • Integrin-dependent tyrosine phosphorylation and growth regulation by Vav
    • Yron I.et al. Integrin-dependent tyrosine phosphorylation and growth regulation by Vav. Cell Adhes. Commun. 7:1999;1-11.
    • (1999) Cell Adhes. Commun. , vol.7 , pp. 1-11
    • Yron, I.1
  • 21
    • 0029960771 scopus 로고    scopus 로고
    • Thrombin receptor activation and integrin engagement stimulate tyrosine phosphorylation of the proto-oncogene product, p95vav, in platelets
    • Cichowski K.et al. Thrombin receptor activation and integrin engagement stimulate tyrosine phosphorylation of the proto-oncogene product, p95vav, in platelets. J. Biol. Chem. 271:1996;7544-7750.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7544-7750
    • Cichowski, K.1
  • 22
    • 0031010040 scopus 로고    scopus 로고
    • Cross-linking of integrins induces tyrosine phosphorylation of the proto-oncogene product Vav and the protein tyrosine kinase Syk in human factor-dependent myeloid cells
    • Gotoh A.et al. Cross-linking of integrins induces tyrosine phosphorylation of the proto-oncogene product Vav and the protein tyrosine kinase Syk in human factor-dependent myeloid cells. Cell Growth Differ. 6:1997;721-729.
    • (1997) Cell Growth Differ. , vol.6 , pp. 721-729
    • Gotoh, A.1
  • 23
    • 0032481142 scopus 로고    scopus 로고
    • Identification of a novel integrin signaling pathway involving the kinase Syk and the guanine nucleotide exchange factor Vav1
    • Miranti C.K.et al. Identification of a novel integrin signaling pathway involving the kinase Syk and the guanine nucleotide exchange factor Vav1. Curr. Biol. 8:1998;1289-1299.
    • (1998) Curr. Biol. , vol.8 , pp. 1289-1299
    • Miranti, C.K.1
  • 24
    • 0032559562 scopus 로고    scopus 로고
    • CAS/Crk coupling serves as a "molecular switch" for induction of cell migration
    • Klemke R.L.et al. CAS/Crk coupling serves as a "molecular switch" for induction of cell migration. J. Cell Biol. 140:1998;961-972.
    • (1998) J. Cell Biol. , vol.140 , pp. 961-972
    • Klemke, R.L.1
  • 25
    • 0032825266 scopus 로고    scopus 로고
    • Regulation of cell contraction and membrane ruffling by distinct signals in migratory cells
    • Cheresh D.A.et al. Regulation of cell contraction and membrane ruffling by distinct signals in migratory cells. J. Cell Biol. 146:1999;1107-1116.
    • (1999) J. Cell Biol. , vol.146 , pp. 1107-1116
    • Cheresh, D.A.1
  • 26
    • 0032544426 scopus 로고    scopus 로고
    • Evidence that DOCK180 up-regulates signals from the CrkII-p130(Cas) complex
    • Kiyokawa E.et al. Evidence that DOCK180 up-regulates signals from the CrkII-p130(Cas) complex. J. Biol. Chem. 273:1998;24479-24484.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24479-24484
    • Kiyokawa, E.1
  • 27
    • 0032213110 scopus 로고    scopus 로고
    • Activation of Rac1 by a Crk SH3-binding protein, DOCK180
    • Kiyokawa E.et al. Activation of Rac1 by a Crk SH3-binding protein, DOCK180. Genes Dev. 12:1998;3331-3336.
    • (1998) Genes Dev. , vol.12 , pp. 3331-3336
    • Kiyokawa, E.1
  • 28
    • 0032523064 scopus 로고    scopus 로고
    • Integrin signaling: The platelet paradigm
    • Shattil S.J.et al. Integrin signaling: the platelet paradigm. Blood. 91:1998;2645-2657.
    • (1998) Blood , vol.91 , pp. 2645-2657
    • Shattil, S.J.1
  • 29
    • 0026700090 scopus 로고
    • A rho gene product in human blood platelets. II. Effects of the ADP-ribosylation by botulinum C3 ADP-ribosyltransferase on platelet aggregation
    • Morii N.et al. A rho gene product in human blood platelets. II. Effects of the ADP-ribosylation by botulinum C3 ADP-ribosyltransferase on platelet aggregation. J. Biol. Chem. 267:1992;20921-20926.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20921-20926
    • Morii, N.1
  • 30
    • 0027471215 scopus 로고
    • Inhibition of PMA-induced, LFA-1-dependent lymphocyte aggregation by ADP ribosylation of the small molecular weight GTP binding protein, rho
    • Tominaga T.et al. Inhibition of PMA-induced, LFA-1-dependent lymphocyte aggregation by ADP ribosylation of the small molecular weight GTP binding protein, rho. J. Cell Biol. 120:1993;1529-1537.
    • (1993) J. Cell Biol. , vol.120 , pp. 1529-1537
    • Tominaga, T.1
  • 31
    • 0030059222 scopus 로고    scopus 로고
    • Role of Rho in chemoattractant-activated leukocyte adhesion through integrins
    • Laudanna C.et al. Role of Rho in chemoattractant-activated leukocyte adhesion through integrins. Science. 271:1996;981-983.
    • (1996) Science , vol.271 , pp. 981-983
    • Laudanna, C.1
  • 32
    • 0032487579 scopus 로고    scopus 로고
    • Adenosine diphosphate (ADP)-ribosylation of the guanosine triphosphatase (GTPase) rho in resting peripheral blood human T lymphocytes results in pseudopodial extension and the inhibition of T cell activation
    • Woodside D.G.et al. Adenosine diphosphate (ADP)-ribosylation of the guanosine triphosphatase (GTPase) rho in resting peripheral blood human T lymphocytes results in pseudopodial extension and the inhibition of T cell activation. J. Exp. Med. 188:1998;1211-1221.
    • (1998) J. Exp. Med. , vol.188 , pp. 1211-1221
    • Woodside, D.G.1
  • 33
    • 0032550177 scopus 로고    scopus 로고
    • Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly
    • Zhong C.et al. Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly. J. Cell. Biol. 141:1998;539-551.
    • (1998) J. Cell. Biol. , vol.141 , pp. 539-551
    • Zhong, C.1
  • 34
    • 0030459360 scopus 로고    scopus 로고
    • Rho is a negative regulator of human monocyte spreading
    • Aepfelbacher M.et al. Rho is a negative regulator of human monocyte spreading. J. Immunol. 157:1996;5070-5075.
    • (1996) J. Immunol. , vol.157 , pp. 5070-5075
    • Aepfelbacher, M.1
  • 35
    • 0031569914 scopus 로고    scopus 로고
    • Cell adhesion in vascular biology. New insights into integrin-ligand interaction
    • Loftus J.C., Liddington R.C. Cell adhesion in vascular biology. New insights into integrin-ligand interaction. J. Clin. Invest. 99:1997;2302-2306.
    • (1997) J. Clin. Invest. , vol.99 , pp. 2302-2306
    • Loftus, J.C.1    Liddington, R.C.2
  • 36
    • 0031952651 scopus 로고    scopus 로고
    • Are changes in integrin affinity and conformation overemphasized?
    • Bazzoni G., Hemler M.E. Are changes in integrin affinity and conformation overemphasized? Trends Biochem. Sci. 23:1998;30-34.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 30-34
    • Bazzoni, G.1    Hemler, M.E.2
  • 37
    • 0032101012 scopus 로고    scopus 로고
    • RhoA and the function of platelet integrin alphaIIbbeta3
    • Leng L.et al. RhoA and the function of platelet integrin alphaIIbbeta3. Blood. 91:1998;4206-4215.
    • (1998) Blood , vol.91 , pp. 4206-4215
    • Leng, L.1
  • 38
    • 0031806711 scopus 로고    scopus 로고
    • Rac regulates integrin-mediated spreading and increased adhesion of T lymphocytes
    • D'Souza-Schorey C.et al. Rac regulates integrin-mediated spreading and increased adhesion of T lymphocytes. Mol. Cell. Biol. 18:1998;3936-3946.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3936-3946
    • D'Souza-Schorey, C.1
  • 39
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes C.D., Hall A. Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell. 81:1995;53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 40
    • 0029562867 scopus 로고
    • The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular rho/rac GTPases
    • Hotchin N.A., Hall A. The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular rho/rac GTPases. J. Cell Biol. 131:1995;1857-1865.
    • (1995) J. Cell Biol. , vol.131 , pp. 1857-1865
    • Hotchin, N.A.1    Hall, A.2
  • 41
    • 0030872949 scopus 로고    scopus 로고
    • Rho- and rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: An essential role for ezrin/radixin/moesin proteins
    • Mackay D.J.G.et al. Rho- and rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: an essential role for ezrin/radixin/moesin proteins. J. Cell Biol. 138:1997;927-938.
    • (1997) J. Cell Biol. , vol.138 , pp. 927-938
    • Mackay, D.J.G.1
  • 42
    • 0033577975 scopus 로고    scopus 로고
    • Interplay between Rac and Rho in the control of substrate contact dynamics
    • Rottner K.et al. Interplay between Rac and Rho in the control of substrate contact dynamics. Curr. Biol. 9:1999;640-648.
    • (1999) Curr. Biol. , vol.9 , pp. 640-648
    • Rottner, K.1
  • 43
    • 0344416986 scopus 로고    scopus 로고
    • Monocyte adhesion and spreading on human endothelial cells is dependent on Rho-regulated receptor clustering
    • Wojciak-Stothard B.et al. Monocyte adhesion and spreading on human endothelial cells is dependent on Rho-regulated receptor clustering. J. Cell Biol. 145:1999;1293-1307.
    • (1999) J. Cell Biol. , vol.145 , pp. 1293-1307
    • Wojciak-Stothard, B.1
  • 44
    • 0033538574 scopus 로고    scopus 로고
    • The immunological synapse: A molecular machine controlling T cell activation
    • Grakoui A.et al. The immunological synapse: a molecular machine controlling T cell activation. Science. 285:1999;221-227.
    • (1999) Science , vol.285 , pp. 221-227
    • Grakoui, A.1
  • 45
    • 0026476697 scopus 로고
    • Focal adhesion kinase (p125FAK): A point of convergence in the action of neuropeptides, integrins, and oncogenes
    • Zachary I., Rozengurt E. Focal adhesion kinase (p125FAK): a point of convergence in the action of neuropeptides, integrins, and oncogenes. Cell. 71:1992;891-894.
    • (1992) Cell , vol.71 , pp. 891-894
    • Zachary, I.1    Rozengurt, E.2
  • 46
    • 0030760119 scopus 로고    scopus 로고
    • Role of integrins in cellular responses to mechanical stress and adhesion
    • Shyy J.Y.J., Chien S. Role of integrins in cellular responses to mechanical stress and adhesion. Curr. Opin. Cell Biol. 9:1997;707-713.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 707-713
    • Shyy, J.Y.J.1    Chien, S.2
  • 47
    • 0032560562 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of paxillin and focal adhesion kinase by activation of muscarinic m3 receptors is dependent on integrin engagement by the extracellular matrix
    • Slack B.E. Tyrosine phosphorylation of paxillin and focal adhesion kinase by activation of muscarinic m3 receptors is dependent on integrin engagement by the extracellular matrix. Proc. Natl. Acad. Sci. U. S. A. 95:1998;7281-7286.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 7281-7286
    • Slack, B.E.1
  • 48
    • 0027496730 scopus 로고
    • ADP-ribosylation of rho p21 inhibits lysophosphatidic acid-induced protein tyrosine phosphorylation and phosphatidylinositol 3-kinase activation in cultured Swiss 3T3 cells
    • Kumagai N.et al. ADP-ribosylation of rho p21 inhibits lysophosphatidic acid-induced protein tyrosine phosphorylation and phosphatidylinositol 3-kinase activation in cultured Swiss 3T3 cells. J. Biol. Chem. 268:1993;24535-24538.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24535-24538
    • Kumagai, N.1
  • 49
    • 0029833712 scopus 로고    scopus 로고
    • Activation of the osmo-sensitive chloride conductance involves P21rho and is accompanied by a transient reorganization of the F-actin cytoskeleton
    • Tilly B.C.et al. Activation of the osmo-sensitive chloride conductance involves P21rho and is accompanied by a transient reorganization of the F-actin cytoskeleton. Mol. Biol. Cell. 7:1996;1419-1427.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1419-1427
    • Tilly, B.C.1
  • 50
    • 0030590084 scopus 로고    scopus 로고
    • Involvement of rho p21 in cyclic strain-induced tyrosine phosphorylation of focal adhesion kinase (pp125FAK), morphological changes and migration of endothelial cells
    • Yano Y.et al. Involvement of rho p21 in cyclic strain-induced tyrosine phosphorylation of focal adhesion kinase (pp125FAK), morphological changes and migration of endothelial cells. Biochem. Biophys. Res. Commun. 224:1996;508-515.
    • (1996) Biochem. Biophys. Res. Commun. , vol.224 , pp. 508-515
    • Yano, Y.1


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