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Volumn 158, Issue 7, 2002, Pages 1287-1297

p21-activated kinase 4 interacts with integrin αvβ5 and regulates αvβ5-mediated cell migration

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA5 INTEGRIN; BETA5 INTEGRIN; CELL PROTEIN; MYOSIN LIGHT CHAIN KINASE; P21 ACTIVATED KINASE 4; PHOSPHOTRANSFERASE; PROTEIN P21; PROTEIN P21 ACTIVATED KINASE 1; UNCLASSIFIED DRUG; VITRONECTIN;

EID: 0037144861     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200207008     Document Type: Article
Times cited : (93)

References (51)
  • 1
    • 0032538973 scopus 로고    scopus 로고
    • PAK4, a novel effector for Cdc42Hs, is implicated in the reorganization of the actin cytoskeleton and in the formation of filopodia
    • Abo, A., J. Qu, M.S. Cammarano, C. Dan, A. Fritsch, V. Baud, B. Belisle, and A. Minden. 1998. PAK4, a novel effector for Cdc42Hs, is implicated in the reorganization of the actin cytoskeleton and in the formation of filopodia. EMBO J 17:6527-6540.
    • (1998) EMBO J. , vol.17 , pp. 6527-6540
    • Abo, A.1    Qu, J.2    Cammarano, M.S.3    Dan, C.4    Fritsch, A.5    Baud, V.6    Belisle, B.7    Minden, A.8
  • 4
    • 0034644537 scopus 로고    scopus 로고
    • Ras and Rho GTPases: A family reunion
    • Bar-Sagi, D., and A. Hall. 2000. Ras and Rho GTPases: a family reunion. Cell. 103:227-238.
    • (2000) Cell , vol.103 , pp. 227-238
    • Bar-Sagi, D.1    Hall, A.2
  • 5
    • 0034865567 scopus 로고    scopus 로고
    • A functional comparison of mutations in integrin β cytoplasmic domains: Effects on the regulation of tyrosine phosphorylation, cell spreading, cell attachment, and β1 integrin conformation
    • Bodeau, A.L., A.L. Berrier, A.M. Mastrangelo, R. Martinez, and S.E. LaFlamme. 2001. A functional comparison of mutations in integrin β cytoplasmic domains: effects on the regulation of tyrosine phosphorylation, cell spreading, cell attachment, and β1 integrin conformation. J. Cell Sci. 114:2795-2807.
    • (2001) J. Cell Sci. , vol.114 , pp. 2795-2807
    • Bodeau, A.L.1    Berrier, A.L.2    Mastrangelo, A.M.3    Martinez, R.4    LaFlamme, S.E.5
  • 6
    • 0028362876 scopus 로고
    • Requirement of vascular integrin αvβ3 for angiogenesis
    • Brooks, P.C., R.A. Clark, and D.A. Cheresh. 1994. Requirement of vascular integrin αvβ3 for angiogenesis. Science. 264:569-571.
    • (1994) Science , vol.264 , pp. 569-571
    • Brooks, P.C.1    Clark, R.A.2    Cheresh, D.A.3
  • 7
    • 0030901145 scopus 로고    scopus 로고
    • Insulin-like growth factor receptor cooperates with integrin αvβ5 to promote tumor cell dissemination in vivo
    • Brooks, P.C., R.L. Klemke, S. Schon, J.M. Lewis, M.A. Schwartz, and D.A. Cheresh. 1997. Insulin-like growth factor receptor cooperates with integrin αvβ5 to promote tumor cell dissemination in vivo. J. Clin. Invest. 99:1390-1398.
    • (1997) J. Clin. Invest. , vol.99 , pp. 1390-1398
    • Brooks, P.C.1    Klemke, R.L.2    Schon, S.3    Lewis, J.M.4    Schwartz, M.A.5    Cheresh, D.A.6
  • 8
    • 0035999990 scopus 로고    scopus 로고
    • Paxillin-dependent paxillin kinase linker and p21-activated kinase localization to focal adhesions involves a multistep activation pathway
    • Brown, M.C., K.A. West, and C.E. Turner. 2002. Paxillin-dependent paxillin kinase linker and p21-activated kinase localization to focal adhesions involves a multistep activation pathway. Mol. Biol. Cell. 13:1550-1565.
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 1550-1565
    • Brown, M.C.1    West, K.A.2    Turner, C.E.3
  • 10
    • 0035943704 scopus 로고    scopus 로고
    • Cytoskeletal changes regulated by the Pak4 serine/threonine kinase are mediated by lim kinase 1 and cofilin
    • Dan, C., A. Kelly, O. Bernard, and A. Minden. 2001a. Cytoskeletal changes regulated by the Pak4 serine/threonine kinase are mediated by lim kinase 1 and cofilin. J. Biol. Chem. 276:32115-32121.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32115-32121
    • Dan, C.1    Kelly, A.2    Bernard, O.3    Minden, A.4
  • 11
    • 0035341895 scopus 로고    scopus 로고
    • The Ste20 group kinases as regulators of MAP kinase cascades
    • Dan, I., N.M. Watanabe, and A. Kusumi. 2001b. The Ste20 group kinases as regulators of MAP kinase cascades. Trends Cell Biol. 11:220-230.
    • (2001) Trends Cell Biol. , vol.11 , pp. 220-230
    • Dan, I.1    Watanabe, N.M.2    Kusumi, A.3
  • 12
    • 0032472918 scopus 로고    scopus 로고
    • Membrane targeting of p21-activated kinase 1 (PAK1) induces neurite outgrowth from PC12 cells
    • Daniels, R.H., P.S. Hall, and G.M. Bokoch. 1998. Membrane targeting of p21-activated kinase 1 (PAK1) induces neurite outgrowth from PC12 cells. EMBO J. 17:754-764.
    • (1998) EMBO J. , vol.17 , pp. 754-764
    • Daniels, R.H.1    Hall, P.S.2    Bokoch, G.M.3
  • 13
    • 0034811439 scopus 로고    scopus 로고
    • p21-activated kinase 1 participates in tracheal smooth muscle cell migration by signaling to p38 Mapk
    • Dechert, M.A., J.M. Holder, and W.T. Gerthoffer. 2001. p21-activated kinase 1 participates in tracheal smooth muscle cell migration by signaling to p38 Mapk. Am. J. Physiol. Cell Physiol. 281:C123-C132.
    • (2001) Am. J. Physiol. Cell Physiol. , vol.281
    • Dechert, M.A.1    Holder, J.M.2    Gerthoffer, W.T.3
  • 14
    • 0033194037 scopus 로고    scopus 로고
    • Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signaling to actin cytoskeletal dynamics
    • Edwards, D.C., L.C. Sandets, G.M. Bokoch, and G.N. Gill. 1999. Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signaling to actin cytoskeletal dynamics. Nat. Cell Biol. 1:253-259.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 253-259
    • Edwards, D.C.1    Sandets, L.C.2    Bokoch, G.M.3    Gill, G.N.4
  • 16
    • 0031749959 scopus 로고    scopus 로고
    • Bodenin: A novel murine gene expressed in restricted areas of the brain
    • Faisst, A.M., and P. Gruss. 1998. Bodenin: a novel murine gene expressed in restricted areas of the brain. Dev. Dyn. 212:293-303.
    • (1998) Dev. Dyn. , vol.212 , pp. 293-303
    • Faisst, A.M.1    Gruss, P.2
  • 19
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signaling
    • Giancotti, F.G., and E. Ruoslahti. 1999. Integrin signaling. Science. 285:1028-1032.
    • (1999) Science , vol.285 , pp. 1028-1032
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 20
    • 0035957986 scopus 로고    scopus 로고
    • The serine/threonine kinase PAK4 prevents caspase activation and protects cells from apoptosis
    • Gnesutta, N., J. Qu, and A. Minden. 2001. The serine/threonine kinase PAK4 prevents caspase activation and protects cells from apoptosis. J . Biol. Chem. 276:14414-14419.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14414-14419
    • Gnesutta, N.1    Qu, J.2    Minden, A.3
  • 22
    • 0029048813 scopus 로고
    • The conserved membrane-proximal region of an integrin cytoplasmic domain specifies ligand binding affinity
    • Hughes, P.E., T.E. O'Toole, J. Ylanne, S.J. Shattil, and M.H. Ginsberg. 1995. The conserved membrane-proximal region of an integrin cytoplasmic domain specifies ligand binding affinity. J. Biol. Chem. 270:12411-12417.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12411-12417
    • Hughes, P.E.1    O'Toole, T.E.2    Ylanne, J.3    Shattil, S.J.4    Ginsberg, M.H.5
  • 23
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes, R.O. 1992. Integrins: versatility, modulation, and signaling in cell adhesion. Cell. 69:11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 24
    • 0031079837 scopus 로고    scopus 로고
    • Changes in the expression of αv integrins in oral squamous cell carcinomas
    • Jones, J., F.M. Watt, and P.M. Speight. 1997. Changes in the expression of αv integrins in oral squamous cell carcinomas. J. Oral Pathol. Med. 26:63-68.
    • (1997) J. Oral Pathol. Med. , vol.26 , pp. 63-68
    • Jones, J.1    Watt, F.M.2    Speight, P.M.3
  • 26
    • 0028043735 scopus 로고
    • Receptor tyrosine kinase signaling required for integrin αvβ5-directed cell motility but not adhesion on vitronectin
    • Klemke, R.L., M. Yebra, E.M. Bayna, and D.A. Cheresh. 1994. Receptor tyrosine kinase signaling required for integrin αvβ5-directed cell motility but not adhesion on vitronectin. J. Cell Biol. 127:859-866.
    • (1994) J. Cell Biol. , vol.127 , pp. 859-866
    • Klemke, R.L.1    Yebra, M.2    Bayna, E.M.3    Cheresh, D.A.4
  • 27
    • 0028260027 scopus 로고
    • A monoclonal antibody inhibits adhesion to fibronectin and vitronectin of a colon carcinoma cell line and recognizes the integrins αvβ3, αvβ5, and αvβ6
    • Lehmann, M., C. Rabenandrasana, R. Tamura, J.C. Lissitzky, V. Quaranta, J. Pichon, and J. Marvaldi. 1994. A monoclonal antibody inhibits adhesion to fibronectin and vitronectin of a colon carcinoma cell line and recognizes the integrins αvβ3, αvβ5, and αvβ6. Cancer Res. 54:2102-2107.
    • (1994) Cancer Res. , vol.54 , pp. 2102-2107
    • Lehmann, M.1    Rabenandrasana, C.2    Tamura, R.3    Lissitzky, J.C.4    Quaranta, V.5    Pichon, J.6    Marvaldi, J.7
  • 28
    • 0034604338 scopus 로고    scopus 로고
    • Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch
    • Lei, M., W. Lu, W. Meng, M.C. Parrini, M.J. Eck, B.J. Mayer, and S.C. Harrison. 2000. Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch. Cell. 102:387-397.
    • (2000) Cell , vol.102 , pp. 387-397
    • Lei, M.1    Lu, W.2    Meng, W.3    Parrini, M.C.4    Eck, M.J.5    Mayer, B.J.6    Harrison, S.C.7
  • 29
    • 0031893954 scopus 로고    scopus 로고
    • Rack1, a receptor for activated protein kinase C, interacts with integrin β subunit
    • Liliental, J., and D.D. Chang. 1998. Rack1, a receptor for activated protein kinase C, interacts with integrin β subunit. J. Biol. Chem. 273:2379-2383.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2379-2383
    • Liliental, J.1    Chang, D.D.2
  • 30
    • 0029805324 scopus 로고    scopus 로고
    • Regulation of phosphorylation pathways by p21 GTPases. The p21 Ras-related Rho subfamily and its role in phosphorylation signalling pathways
    • Lim, L., E. Manser, T. Leung, and C. Hall. 1996. Regulation of phosphorylation pathways by p21 GTPases. The p21 Ras-related Rho subfamily and its role in phosphorylation signalling pathways. Eur. J. Biochem. 242:171-185.
    • (1996) Eur. J. Biochem. , vol.242 , pp. 171-185
    • Lim, L.1    Manser, E.2    Leung, T.3    Hall, C.4
  • 31
    • 0035805633 scopus 로고    scopus 로고
    • Association of the membrane proximal regions of the α and β subunit cytoplasmic domains constrains an integrin in the inactive state
    • Lu, C., J. Takagi, and T.A. Springer. 2001. Association of the membrane proximal regions of the α and β subunit cytoplasmic domains constrains an integrin in the inactive state. J. Biol. Chem. 276:14642-14648.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14642-14648
    • Lu, C.1    Takagi, J.2    Springer, T.A.3
  • 32
    • 0031080595 scopus 로고    scopus 로고
    • Activation of Pak by membrane localization mediated by an SH3 domain from the adaptor protein Nck
    • Lu, W., S. Katz, R. Gupta, and B.J. Mayer. 1997. Activation of Pak by membrane localization mediated by an SH3 domain from the adaptor protein Nck. Curr. Biol. 7:85-94.
    • (1997) Curr. Biol. , vol.7 , pp. 85-94
    • Lu, W.1    Katz, S.2    Gupta, R.3    Mayer, B.J.4
  • 33
    • 0031036626 scopus 로고    scopus 로고
    • Expression of constitutively active α-PAK reveals effects of the kinase on actin and focal complexes
    • Manser, E., H.Y. Huang, T.H. Loo, X.Q. Chen, J.M. Dong, T. Leung, and L. Lim. 1997. Expression of constitutively active α-PAK reveals effects of the kinase on actin and focal complexes. Mol. Cell. Biol. 17:1129-1143.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1129-1143
    • Manser, E.1    Huang, H.Y.2    Loo, T.H.3    Chen, X.Q.4    Dong, J.M.5    Leung, T.6    Lim, L.7
  • 34
    • 0035503218 scopus 로고    scopus 로고
    • Dok-R plays a pivotal role in angiopoietn-1-dependent cell migration through recruitment and activation of Pak
    • Master, Z., N. Jones, J. Tran, J. Jones, R.S. Kerbel, and D.J. Dumont. 2001. Dok-R plays a pivotal role in angiopoietn-1-dependent cell migration through recruitment and activation of Pak. EMBO J. 20:5919-5928.
    • (2001) EMBO J. , vol.20 , pp. 5919-5928
    • Master, Z.1    Jones, N.2    Tran, J.3    Jones, J.4    Kerbel, R.S.5    Dumont, D.J.6
  • 35
    • 0032488053 scopus 로고    scopus 로고
    • A protein related to p21-activated kinase (PAK) that is involved in neurogenesis in the Drosophila adult central nervous system
    • Melzig, J., K.H. Rein, U. Schafer, H. Pfister, H. Jackle, M. Heisenberg, and T. Raabe. 1998. A protein related to p21-activated kinase (PAK) that is involved in neurogenesis in the Drosophila adult central nervous system. Curr. Biol. 8:1223-1226.
    • (1998) Curr. Biol. , vol.8 , pp. 1223-1226
    • Melzig, J.1    Rein, K.H.2    Schafer, U.3    Pfister, H.4    Jackle, H.5    Heisenberg, M.6    Raabe, T.7
  • 36
    • 0029148903 scopus 로고
    • Conserved regions in the cytoplasmic domains of the leukocyte integrin αLβ2 are involved in endoplasmic reticulum retention, dimerization, and cytoskeletal association
    • Pardi, R., G. Bossi, L. Inverardi, E. Rovida, and J.R. Bender. 1995. Conserved regions in the cytoplasmic domains of the leukocyte integrin αLβ2 are involved in endoplasmic reticulum retention, dimerization, and cytoskeletal association. J. Immunol. 155:1252-1263.
    • (1995) J. Immunol. , vol.155 , pp. 1252-1263
    • Pardi, R.1    Bossi, G.2    Inverardi, L.3    Rovida, E.4    Bender, J.R.5
  • 37
    • 0034595381 scopus 로고    scopus 로고
    • Adhesion to the extracellular matrix regulates the coupling of the small GTP-ase Rac to its effector PAK
    • del Pozo, M.A., L.S. Price, N.B. Alderson, X.D. Ren, and M.A. Schwartz. 2000. Adhesion to the extracellular matrix regulates the coupling of the small GTP-ase Rac to its effector PAK. EMBO J. 19:2008-2014.
    • (2000) EMBO J. , vol.19 , pp. 2008-2014
    • Del Pozo, M.A.1    Price, L.S.2    Alderson, N.B.3    Ren, X.D.4    Schwartz, M.A.5
  • 38
    • 0031844821 scopus 로고    scopus 로고
    • Activation of Rac and Cdc42 by integrins mediates cell spreading
    • Price, L.S., J. Leng, M.A. Schwartz, and G.M. Bokoch. 1998. Activation of Rac and Cdc42 by integrins mediates cell spreading. Mol. Biol. Cell. 9:1863-1871.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1863-1871
    • Price, L.S.1    Leng, J.2    Schwartz, M.A.3    Bokoch, G.M.4
  • 40
    • 0025248597 scopus 로고
    • Cloning, primary structure and properties of a novel human integrin β subunit
    • Ramaswamy, H., and M.E. Hemler. 1990. Cloning, primary structure and properties of a novel human integrin β subunit. EMBO J. 9:1561-1568.
    • (1990) EMBO J. , vol.9 , pp. 1561-1568
    • Ramaswamy, H.1    Hemler, M.E.2
  • 41
    • 0033605738 scopus 로고    scopus 로고
    • Inhibition of myosin light chain kinase by p21-activated kinase
    • Sanders, L.C., F. Matsumura, G.M. Bokoch, and P. de Lanerolle. 1999. Inhibition of myosin light chain kinase by p21-activated kinase. Science. 283:2083-2085.
    • (1999) Science , vol.283 , pp. 2083-2085
    • Sanders, L.C.1    Matsumura, F.2    Bokoch, G.M.3    De Lanerolle, P.4
  • 44
    • 0033577902 scopus 로고    scopus 로고
    • p21-activated kinase 1 (Pak1) regulates cell motility in mammalian fibroblasts
    • Sells, M.A., J.T. Boyd, and J. Chernoff. 1999. p21-activated kinase 1 (Pak1) regulates cell motility in mammalian fibroblasts. J. Cell Biol. 145:837-849.
    • (1999) J. Cell Biol. , vol.145 , pp. 837-849
    • Sells, M.A.1    Boyd, J.T.2    Chernoff, J.3
  • 46
    • 0030038229 scopus 로고    scopus 로고
    • Suppression of p53 activity and p21WAF1/CIP1 expression by vascular cell integrin αVβ3 during angiogenesis
    • Strömblad, S., J.C. Becker, M. Yebra, P.C. Brooks, and D.A. Cheresh. 1996. Suppression of p53 activity and p21WAF1/CIP1 expression by vascular cell integrin αVβ3 during angiogenesis. J. Clin. Invest. 98:426-433.
    • (1996) J. Clin. Invest. , vol.98 , pp. 426-433
    • Strömblad, S.1    Becker, J.C.2    Yebra, M.3    Brooks, P.C.4    Cheresh, D.A.5
  • 47
    • 0025895086 scopus 로고
    • Integrins αvβ3 and αvβ5 contribute to cell attachment to vitronectin but differentially distribute on the cell surface
    • Wayner, E.A., R.A. Orlando, and D.A. Cheresh. 1991. Integrins αvβ3 and αvβ5 contribute to cell attachment to vitronectin but differentially distribute on the cell surface. J. Cell Biol. 113:919-929.
    • (1991) J. Cell Biol. , vol.113 , pp. 919-929
    • Wayner, E.A.1    Orlando, R.A.2    Cheresh, D.A.3
  • 49
    • 0029847191 scopus 로고    scopus 로고
    • Requirement of receptor-bound urokinase-type plasminogen activator for integrin αvβ5-directed cell migration
    • Yebra, M., G.C. Parry, S. Strömblad, N. Mackman, S. Rosenberg, B.M. Mueller, and D.A. Cheresh. 1996. Requirement of receptor-bound urokinase-type plasminogen activator for integrin αvβ5-directed cell migration. J. Biol. Chem. 271:29393-29399.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29393-29399
    • Yebra, M.1    Parry, G.C.2    Strömblad, S.3    Mackman, N.4    Rosenberg, S.5    Mueller, B.M.6    Cheresh, D.A.7
  • 51
    • 0031659894 scopus 로고    scopus 로고
    • The membrane proximal region of the integrin β cytoplasmic domain can mediate oligometization
    • Zage, P.E., and E.E. Marcantonio. 1998. The membrane proximal region of the integrin β cytoplasmic domain can mediate oligometization. Cell Adhes. Commun. 5:335-347.
    • (1998) Cell Adhes. Commun. , vol.5 , pp. 335-347
    • Zage, P.E.1    Marcantonio, E.E.2


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