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Volumn 167, Issue 1, 2004, Pages 111-122

Rap1 promotes cell spreading by localizing Rac guanine nucleotide exchange factors

Author keywords

[No Author keywords available]

Indexed keywords

COOL 1 PROTEIN; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE TRIPHOSPHATASE; INTEGRIN; RAC PROTEIN; RAC1 PROTEIN; RAP PROTEIN; RAP1 PROTEIN; RAS PROTEIN; SWAP70 PROTEIN; TIAM1 PROTEIN; UNCLASSIFIED DRUG; VAV2 PROTEIN;

EID: 5444230311     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200404068     Document Type: Article
Times cited : (221)

References (54)
  • 1
    • 0037351084 scopus 로고    scopus 로고
    • Vav1 transduces TCR signals required for LFA-1 function and cell polarization at the immunological synapse
    • Ardouin, L., M. Bracke, A. Mathiot, S.N. Pagakis, T. Norton, N. Hogg, and V.L. Tybulewicz. 2003. Vav1 transduces TCR signals required for LFA-1 function and cell polarization at the immunological synapse. Eur. J. Immunol. 33:790-797.
    • (2003) Eur. J. Immunol. , vol.33 , pp. 790-797
    • Ardouin, L.1    Bracke, M.2    Mathiot, A.3    Pagakis, S.N.4    Norton, T.5    Hogg, N.6    Tybulewicz, V.L.7
  • 2
    • 0033081407 scopus 로고    scopus 로고
    • The Rap1 GTPase functions as a regulator of morphogenesis in vivo
    • Asha, H., N.D. de Ruiter, M.G. Wang, and LK. Hariharan. 1999. The Rap1 GTPase functions as a regulator of morphogenesis in vivo. EMBO J. 18:605-615.
    • (1999) EMBO J. , vol.18 , pp. 605-615
    • Asha, H.1    De Ruiter, N.D.2    Wang, M.G.3    Hariharan, L.K.4
  • 3
    • 0034213327 scopus 로고    scopus 로고
    • Rho GTPases and their effector proteins
    • Bishop, A.L., and A. Hall. 2000. Rho GTPases and their effector proteins. Biochem. J. 348:241-255.
    • (2000) Biochem. J. , vol.348 , pp. 241-255
    • Bishop, A.L.1    Hall, A.2
  • 5
    • 0034254923 scopus 로고    scopus 로고
    • The junctional multidomain protein AF-6 is a binding partner of the Rap1 A GTPase and associates with the actin cytoskeletal regulator profilin
    • Boettner, B., E.E. Govek, J. Cross, and L. Van Aelst. 2000. The junctional multidomain protein AF-6 is a binding partner of the Rap1 A GTPase and associates with the actin cytoskeletal regulator profilin. Proc. Natl. Acad. Sci. USA. 97:9064-9069.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9064-9069
    • Boettner, B.1    Govek, E.E.2    Cross, J.3    Van Aelst, L.4
  • 6
    • 0036210706 scopus 로고    scopus 로고
    • Critical but distinct roles for the pleckstrin homology and cysteine-rich domains as positive modulators of Vav2 signaling and transformation
    • Booden, M.A., S.L. Campbell, and C.J. Der. 2002. Critical but distinct roles for the pleckstrin homology and cysteine-rich domains as positive modulators of Vav2 signaling and transformation. Mol. Cell. Biol. 22:2487-2497.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2487-2497
    • Booden, M.A.1    Campbell, S.L.2    Der, C.J.3
  • 8
    • 1442331993 scopus 로고    scopus 로고
    • Integrin activation
    • Calderwood, D.A. 2004. Integrin activation. J. Cell Sci. 117:657-666.
    • (2004) J. Cell Sci. , vol.117 , pp. 657-666
    • Calderwood, D.A.1
  • 10
    • 0037329747 scopus 로고    scopus 로고
    • Cellular functions of the Rap1 GTP-binding protein: A pattern emerges
    • Caron, E. 2003. Cellular functions of the Rap1 GTP-binding protein: a pattern emerges. J. Cell Sci. 116:435-440.
    • (2003) J. Cell Sci. , vol.116 , pp. 435-440
    • Caron, E.1
  • 11
    • 0041356888 scopus 로고    scopus 로고
    • Rheb binds tuberous sclerosis complex 2 (TSC2) and promotes S6 kinase activation in a rapamycin- and farnesylation-dependent manner
    • Castro, A.F., J.F. Rebhun, G.J. Clark, and L.A. Quilliam. 2003. Rheb binds tuberous sclerosis complex 2 (TSC2) and promotes S6 kinase activation in a rapamycin- and farnesylation-dependent manner. J. Biol. Chem. 278:32493-32496.
    • (2003) J. Biol. Chem. , vol.278 , pp. 32493-32496
    • Castro, A.F.1    Rebhun, J.F.2    Clark, G.J.3    Quilliam, L.A.4
  • 12
    • 0037128213 scopus 로고    scopus 로고
    • Purification of pseudopodia from polarized cells reveals redistribution and activation of Rac through assembly of a CAS/Crk scaffold
    • Cho, S.Y., and R.L. Klemke. 2002. Purification of pseudopodia from polarized cells reveals redistribution and activation of Rac through assembly of a CAS/Crk scaffold. J. Cell Biol. 156:725-736.
    • (2002) J. Cell Biol. , vol.156 , pp. 725-736
    • Cho, S.Y.1    Klemke, R.L.2
  • 13
    • 0034595381 scopus 로고    scopus 로고
    • Adhesion to the extracellular matrix regulates the coupling of the small GTPase 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 GTPase 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
  • 14
    • 0037220769 scopus 로고    scopus 로고
    • Guanine exchange-dependent and -independent effects of Vav1 on integrin-induced T cell spreading
    • del Pozo, M.A., M.A. Schwartz, J. Hu, W.B. Kiosses, A. Altman, and M. Villalba. 2003. Guanine exchange-dependent and -independent effects of Vav1 on integrin-induced T cell spreading. J. Immunol. 170:41-47.
    • (2003) J. Immunol. , vol.170 , pp. 41-47
    • Del Pozo, M.A.1    Schwartz, M.A.2    Hu, J.3    Kiosses, W.B.4    Altman, A.5    Villalba, M.6
  • 15
    • 0030741294 scopus 로고    scopus 로고
    • Immunolocalization of rap1 in the rat parotid gland: Detection on secretory granule membranes
    • D'Silva, N.J., D.H. DiJulio, C.M. Belton, K.L. Jacobson, and E.L. Watson. 1997. Immunolocalization of rap1 in the rat parotid gland: detection on secretory granule membranes. J. Histochem. Cytochem. 45:965-973.
    • (1997) J. Histochem. Cytochem. , vol.45 , pp. 965-973
    • D'Silva, N.J.1    DiJulio, D.H.2    Belton, C.M.3    Jacobson, K.L.4    Watson, E.L.5
  • 17
    • 0035118704 scopus 로고    scopus 로고
    • Temporal and spatial regulation of Rho-type guanine-nucleotide exchange factors: The yeast perspective
    • Gulli, M.P., and M. Peter. 2001. Temporal and spatial regulation of Rho-type guanine-nucleotide exchange factors: the yeast perspective. Genes Dev. 15:365-379.
    • (2001) Genes Dev. , vol.15 , pp. 365-379
    • Gulli, M.P.1    Peter, M.2
  • 18
    • 15144353776 scopus 로고    scopus 로고
    • Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav
    • Han, J., K. Luby-Phelps, B. Das, X. Shu, Y. Xia, R.D. Mosteller, U.M. Krishna, J.R. Falck, M.A. White, and D. Broek. 1998. Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav. Science. 279:558-560.
    • (1998) Science , vol.279 , pp. 558-560
    • Han, J.1    Luby-Phelps, K.2    Das, B.3    Shu, X.4    Xia, Y.5    Mosteller, R.D.6    Krishna, U.M.7    Falck, J.R.8    White, M.A.9    Broek, D.10
  • 19
    • 0037542854 scopus 로고    scopus 로고
    • Ras proteins: Different signals from different locations
    • Hancock, J.F. 2003. Ras proteins: different signals from different locations. Nat. Rev. Mol. Cell Biol. 4:373-384.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 373-384
    • Hancock, J.F.1
  • 20
    • 0025932448 scopus 로고
    • The Drosophila roughened mutation: Activation of a rap homolog disrupts eye development and interferes with cell determination
    • Hariharan, I.K., R.W. Carthew, and G.M. Rubin. 1991. The Drosophila roughened mutation: activation of a rap homolog disrupts eye development and interferes with cell determination. Cell. 67:717-722.
    • (1991) Cell , vol.67 , pp. 717-722
    • Hariharan, I.K.1    Carthew, R.W.2    Rubin, G.M.3
  • 21
    • 0029587739 scopus 로고
    • Cysteine-rich region of Raf-1 interacts with activator domain of post-translationally modified Ha-Ras
    • Hu, C.D., K. Kariya, M. Tamada, K. Akasaka, M. Shirouzu, S. Yokoyama, and T. Kataoka. 1995. Cysteine-rich region of Raf-1 interacts with activator domain of post-translationally modified Ha-Ras. J. Biol. Chem. 270:30274-30277.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30274-30277
    • Hu, C.D.1    Kariya, K.2    Tamada, M.3    Akasaka, K.4    Shirouzu, M.5    Yokoyama, S.6    Kataoka, T.7
  • 22
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes, R.O. 2002. Integrins: bidirectional, allosteric signaling machines. Cell. 110:673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 23
    • 0042490495 scopus 로고    scopus 로고
    • RAPL, a Rap1-binding molecule that mediates Rap1-induced adhesion through spatial regulation of LFA-1
    • Katagiri, K., A. Maeda, M. Shimonaka, and T. Kinashi. 2003. RAPL, a Rap1-binding molecule that mediates Rap1-induced adhesion through spatial regulation of LFA-1. Nat. Immunol. 4:741-748.
    • (2003) Nat. Immunol. , vol.4 , pp. 741-748
    • Katagiri, K.1    Maeda, A.2    Shimonaka, M.3    Kinashi, T.4
  • 25
    • 0024600222 scopus 로고
    • A ras-related gene with transformation suppressor activity
    • Kitayama, H., Y. Sugimoto, T. Matsuzaki, Y. Ikawa, and M. Noda. 1989. A ras-related gene with transformation suppressor activity. Cell. 56:77-84.
    • (1989) Cell , vol.56 , pp. 77-84
    • Kitayama, H.1    Sugimoto, Y.2    Matsuzaki, T.3    Ikawa, Y.4    Noda, M.5
  • 26
    • 0037083415 scopus 로고    scopus 로고
    • Rap1 GTPase regulation of adherens junction positioning and cell adhesion
    • Knox, A.L., and N.H. Brown. 2002. Rap1 GTPase regulation of adherens junction positioning and cell adhesion. Science. 295:1285-1288.
    • (2002) Science , vol.295 , pp. 1285-1288
    • Knox, A.L.1    Brown, N.H.2
  • 29
    • 0033826334 scopus 로고    scopus 로고
    • Vav2 activates Rac1, Cdc42, and RhoA down-stream from growth factor receptors but not β1 integrins
    • Liu, B.P., and K. Burridge. 2000. Vav2 activates Rac1, Cdc42, and RhoA down-stream from growth factor receptors but not β1 integrins. Mol. Cell. Biol. 20:7160-7169.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7160-7169
    • Liu, B.P.1    Burridge, K.2
  • 30
    • 0031830195 scopus 로고    scopus 로고
    • Cytoskeletal reorganization by G protein-coupled receptors is dependent on phosphoinositide 3-kinase γ, a Rac guanosine exchange factor, and Rac
    • Ma, A.D., A. Metjian, S. Bagrodia, S. Taylor, and C.S. Abrams. 1998. Cytoskeletal reorganization by G protein-coupled receptors is dependent on phosphoinositide 3-kinase γ, a Rac guanosine exchange factor, and Rac. Mol. Cell. Biol. 18:4744-1751.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4744-1751
    • Ma, A.D.1    Metjian, A.2    Bagrodia, S.3    Taylor, S.4    Abrams, C.S.5
  • 32
    • 0344885558 scopus 로고    scopus 로고
    • Structural evidence for feedback activation by Ras.GTP of the Ras-specific nucleotide exchange factor SOS
    • Margarit, S.M., H. Sondermann, B.E. Hall, B. Nagar, A. Hoelz, M. Pirruccello, D. Bar-Sagi, and J. Kuriyan. 2003. Structural evidence for feedback activation by Ras.GTP of the Ras-specific nucleotide exchange factor SOS. Cell. 112:685-695.
    • (2003) Cell , vol.112 , pp. 685-695
    • Margarit, S.M.1    Sondermann, H.2    Hall, B.E.3    Nagar, B.4    Hoelz, A.5    Pirruccello, M.6    Bar-Sagi, D.7    Kuriyan, J.8
  • 33
    • 0035833248 scopus 로고    scopus 로고
    • Vav2 is required for cell spreading
    • Marignani, P.A., and C.L. Carpenter. 2001. Vav2 is required for cell spreading. J. Cell Biol. 154:177-186.
    • (2001) J. Cell Biol. , vol.154 , pp. 177-186
    • Marignani, P.A.1    Carpenter, C.L.2
  • 34
    • 0035825193 scopus 로고    scopus 로고
    • Differential localization of Rho GTPases in live cells: Regulation by hypervariable regions and RhoGDI binding
    • Michaelson, D., J. Silletti, G. Murphy, P. D'Eustachio, M. Rush, and M.R. Philips. 2001. Differential localization of Rho GTPases in live cells: regulation by hypervariable regions and RhoGDI binding. J. Cell Biol. 152:111-126.
    • (2001) J. Cell Biol. , vol.152 , pp. 111-126
    • Michaelson, D.1    Silletti, J.2    Murphy, G.3    D'Eustachio, P.4    Rush, M.5    Philips, M.R.6
  • 35
    • 1642341451 scopus 로고    scopus 로고
    • Talin: An emerging focal point of adhesion dynamics
    • Nayal, A., D.J. Webb, and A.F. Horwitz. 2004. Talin: an emerging focal point of adhesion dynamics. Curr. Opin. Cell Biol. 16:94-98.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 94-98
    • Nayal, A.1    Webb, D.J.2    Horwitz, A.F.3
  • 37
    • 0030940119 scopus 로고    scopus 로고
    • Two active states of the Ras-related Bud1/Rsr1 protein bind to different effectors to determine yeast cell polarity
    • Park, H.O., E. Bi, J.R. Pringle, and I. Herskowitz. 1997. Two active states of the Ras-related Bud1/Rsr1 protein bind to different effectors to determine yeast cell polarity. Proc. Natl. Acad. Sci. USA. 94:4463-4468.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4463-4468
    • Park, H.O.1    Bi, E.2    Pringle, J.R.3    Herskowitz, I.4
  • 38
    • 0037178792 scopus 로고    scopus 로고
    • Localization of the Rsr1/Bud1 GTPase involved in selection of a proper growth site in yeast
    • Park, H.O., PJ. Rang, and A.W. Rachfal. 2002. Localization of the Rsr1/Bud1 GTPase involved in selection of a proper growth site in yeast. J. Biol. Chem. 277:26721-26724.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26721-26724
    • Park, H.O.1    Rang, P.J.2    Rachfal, A.W.3
  • 39
    • 0028246501 scopus 로고
    • Association of Rap1a and Rap1b proteins with late endocytic/phagocytic compartments and Rap2a with the Golgi complex
    • Pizon, V., M. Desjardins, C. Bucci, R.G. Parton, and M. Zerial. 1994. Association of Rap1a and Rap1b proteins with late endocytic/phagocytic compartments and Rap2a with the Golgi complex. J. Cell Sci. 107:1661-1670.
    • (1994) J. Cell Sci. , vol.107 , pp. 1661-1670
    • Pizon, V.1    Desjardins, M.2    Bucci, C.3    Parton, R.G.4    Zerial, M.5
  • 40
    • 0036364408 scopus 로고    scopus 로고
    • A growing family of guanine nucleotide exchange factors is responsible for activation of Ras-family GTPases
    • Quilliam, L.A., J.F. Rebhun, and A.F. Castro. 2002. A growing family of guanine nucleotide exchange factors is responsible for activation of Ras-family GTPases. Prog. Nucleic Acid Res. Mol. Biol. 71:391-444.
    • (2002) Prog. Nucleic Acid Res. Mol. Biol. , vol.71 , pp. 391-444
    • Quilliam, L.A.1    Rebhun, J.F.2    Castro, A.F.3
  • 41
    • 0026551586 scopus 로고
    • Subcellular distribution of the Rap1A protein in human neutrophils: Colocalization and cotranslocation with cytochrome b559
    • Quinn, M.T., M.L. Mullen, A.J. Jesaitis, and J.G. Linner. 1992. Subcellular distribution of the Rap1A protein in human neutrophils: colocalization and cotranslocation with cytochrome b559. Blood. 79:1563-1573.
    • (1992) Blood , vol.79 , pp. 1563-1573
    • Quinn, M.T.1    Mullen, M.L.2    Jesaitis, A.J.3    Linner, J.G.4
  • 42
    • 0032900498 scopus 로고    scopus 로고
    • ARF6 requirement for Rac ruffling suggests a role for membrane trafficking in cortical actin rearrangements
    • Radhakrishna, H., O. Al-Awar, Z. Khachikian, and J.G. Donaldson. 1999. ARF6 requirement for Rac ruffling suggests a role for membrane trafficking in cortical actin rearrangements. J. Cell Sci. 112:855-866.
    • (1999) J. Cell Sci. , vol.112 , pp. 855-866
    • Radhakrishna, H.1    Al-Awar, O.2    Khachikian, Z.3    Donaldson, J.G.4
  • 45
    • 0036644975 scopus 로고    scopus 로고
    • Guanine nucleotide exchange factors for Rho GTPases: Turning on the switch
    • Schmidt, A., and A. Hall. 2002. Guanine nucleotide exchange factors for Rho GTPases: turning on the switch. Genes Dev. 16:1587-1609.
    • (2002) Genes Dev. , vol.16 , pp. 1587-1609
    • Schmidt, A.1    Hall, A.2
  • 46
    • 0032538792 scopus 로고    scopus 로고
    • Phosphorylation-dependent and constitutive activation of Rho proteins by wild-type and oncogenic Vav-2
    • Schuebel, K.E., N. Movilla, J.L. Rosa, and X.R. Bustelo. 1998. Phosphorylation-dependent and constitutive activation of Rho proteins by wild-type and oncogenic Vav-2. EMBO J. 17:6608-6621.
    • (1998) EMBO J. , vol.17 , pp. 6608-6621
    • Schuebel, K.E.1    Movilla, N.2    Rosa, J.L.3    Bustelo, X.R.4
  • 48
    • 0038741814 scopus 로고    scopus 로고
    • Does Rap1 deserve a bad Rap?
    • Stork, P.J. 2003. Does Rap1 deserve a bad Rap? Trends Biochem. Sci. 28:267-275.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 267-275
    • Stork, P.J.1
  • 50
    • 0035016611 scopus 로고    scopus 로고
    • Coordinated regulation of Rap1 and thyroid differentiation by cyclic AMP and protein kinase A
    • Tsygankova, O.M., A. Saavedra, J.F. Rebhun, L.A. Quilliam, and J.L. Meinkoth. 2001. Coordinated regulation of Rap1 and thyroid differentiation by cyclic AMP and protein kinase A. Mol. Cell. Biol. 21:1921-1929.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1921-1929
    • Tsygankova, O.M.1    Saavedra, A.2    Rebhun, J.F.3    Quilliam, L.A.4    Meinkoth, J.L.5
  • 52
    • 0037262297 scopus 로고    scopus 로고
    • The guanine nucleotide exchange factor C3G is necessary for the formation of focal adhesions and vascular maturation
    • Voss, A.K., P. Gruss, and T. Thomas. 2003. The guanine nucleotide exchange factor C3G is necessary for the formation of focal adhesions and vascular maturation. Development. 130:355-367.
    • (2003) Development , vol.130 , pp. 355-367
    • Voss, A.K.1    Gruss, P.2    Thomas, T.3
  • 54
    • 0033604512 scopus 로고    scopus 로고
    • Ras and Rap1: Two highly related small GTPases with distinct function
    • Zwartkruis, F.J., and J.L. Bos. 1999. Ras and Rap1: two highly related small GTPases with distinct function. Exp. Cell Res. 253:157-165.
    • (1999) Exp. Cell Res. , vol.253 , pp. 157-165
    • Zwartkruis, F.J.1    Bos, J.L.2


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