메뉴 건너뛰기




Volumn 164, Issue 3, 2004, Pages 461-470

Rap1 up-regulation and activation on plasma membrane regulates T cell adhesion

Author keywords

Endosomes; GFP; GTPase; Jurkat; Ras

Indexed keywords

GREEN FLUORESCENT PROTEIN; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; INTEGRIN; MITOGENIC AGENT; RAP PROTEIN; RAS PROTEIN;

EID: 0842266583     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200311093     Document Type: Article
Times cited : (147)

References (45)
  • 1
    • 0032560506 scopus 로고    scopus 로고
    • Mitogenic and oncogenic properties of the small G protein Rap1b
    • Altschuler, D.L., and F. Ribeiro-Neto. 1998. Mitogenic and oncogenic properties of the small G protein Rap1b. Proc. Natl. Acad. Sci. USA. 95:7475-7479.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7475-7479
    • Altschuler, D.L.1    Ribeiro-Neto, F.2
  • 2
    • 0026031577 scopus 로고
    • Association of the Ras-antagonistic Rap1/Krev-1 proteins with the Golgi complex
    • Beranger, F., B. Goud, A. Tavitian, and J. de Gunzburg. 1991. Association of the Ras-antagonistic Rap1/Krev-1 proteins with the Golgi complex. Proc. Natl. Acad. Sci. USA. 88:1606-1610.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1606-1610
    • Beranger, F.1    Goud, B.2    Tavitian, A.3    De Gunzburg, J.4
  • 3
    • 0028079846 scopus 로고
    • Ultrastructural localization of the small GTP-binding protein Rap1 in human platelets and megakaryocytes
    • Berger, G., R. Quarck, D. Tenza, S. Levy-Toledano, J. de Gunzburg, and E.M. Cramer. 1994. Ultrastructural localization of the small GTP-binding protein Rap1 in human platelets and megakaryocytes. Br. J. Haematol. 88:372-382.
    • (1994) Br. J. Haematol. , vol.88 , pp. 372-382
    • Berger, G.1    Quarck, R.2    Tenza, D.3    Levy-Toledano, S.4    De Gunzburg, J.5    Cramer, E.M.6
  • 4
    • 0032401757 scopus 로고    scopus 로고
    • All in the family? New insights and questions regarding interconnectivity of Ras, Rap1 and Ral
    • Bos, J.L. 1998. All in the family? New insights and questions regarding interconnectivity of Ras, Rap1 and Ral. EMBO J. 17:6776-6782.
    • (1998) EMBO J. , vol.17 , pp. 6776-6782
    • Bos, J.L.1
  • 9
    • 0031055415 scopus 로고    scopus 로고
    • Minimal Ras-binding domain of Raf1 can be used as an activation-specific probe for Ras
    • de Rooij, J. and J.L. Bos. 1997. Minimal Ras-binding domain of Raf1 can be used as an activation-specific probe for Ras. Oncogene. 14:623-5.
    • (1997) Oncogene , vol.14 , pp. 623-625
    • De Rooij, J.1    Bos, J.L.2
  • 10
    • 0036789949 scopus 로고    scopus 로고
    • Ras and relatives - Job sharing and networking keep an old family together
    • Ehrhardt, A., G.R. Ehrhardt, X. Guo, and J.W. Schrader. 2002. Ras and relatives - job sharing and networking keep an old family together. Exp. Hematol. 30:1089-1106.
    • (2002) Exp. Hematol. , vol.30 , pp. 1089-1106
    • Ehrhardt, A.1    Ehrhardt, G.R.2    Guo, X.3    Schrader, J.W.4
  • 12
    • 0028291894 scopus 로고
    • Tetanus toxin-mediated cleavage of cellubrevin impairs exocytosis of transferrin receptor-containing vesicles in CHO cells
    • Galli, T., T. Chilcote, O. Mundigl, T. Binz, H. Niemann, and P. De Camilli. 1994. Tetanus toxin-mediated cleavage of cellubrevin impairs exocytosis of transferrin receptor-containing vesicles in CHO cells. J. Cell Biol. 125:1015-1024.
    • (1994) J. Cell Biol. , vol.125 , pp. 1015-1024
    • Galli, T.1    Chilcote, T.2    Mundigl, O.3    Binz, T.4    Niemann, H.5    De Camilli, P.6
  • 13
    • 0035834649 scopus 로고    scopus 로고
    • Identification and characterization of RA-GEF-2, a Rap guanine nucleotide exchange factor that serves as a downstream target of M-Ras
    • Gao, X., T. Satoh, Y. Liao, C. Song, C.D. Hu, K. Kariya Ki, and T. Kataoka. 2001. Identification and characterization of RA-GEF-2, a Rap guanine nucleotide exchange factor that serves as a downstream target of M-Ras. J. Biol. Chem. 276:42219-42225.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42219-42225
    • Gao, X.1    Satoh, T.2    Liao, Y.3    Song, C.4    Hu, C.D.5    Kariya Ki, K.6    Kataoka, T.7
  • 15
    • 0026037624 scopus 로고
    • A CAAX or a CAAL motif and a second signal are sufficient for plasma membrane targeting of ras proteins
    • Hancock, J.F., K. Cadwallader, H. Paterson, and C.J. Marshall. 1991. A CAAX or a CAAL motif and a second signal are sufficient for plasma membrane targeting of ras proteins. EMBO J. 10:4033-4039.
    • (1991) EMBO J. , vol.10 , pp. 4033-4039
    • Hancock, J.F.1    Cadwallader, K.2    Paterson, H.3    Marshall, C.J.4
  • 16
    • 0029913467 scopus 로고    scopus 로고
    • Differential interaction of the ras family GTP-binding proteins H-Ras, Rap1, and R-Ras with the putative effector molecules Raf kinase and Ral-guanine nucleotide exchange factor
    • Herrmann, C., G. Horn, M. Spaargaren, and A. Wittinghofer. 1996. Differential interaction of the ras family GTP-binding proteins H-Ras, Rap1, and R-Ras with the putative effector molecules Raf kinase and Ral-guanine nucleotide exchange factor. J. Biol. Chem. 271:6794-6800.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6794-6800
    • Herrmann, C.1    Horn, G.2    Spaargaren, M.3    Wittinghofer, A.4
  • 17
    • 0036146452 scopus 로고    scopus 로고
    • Rap1 functions as a key regulator of T-cell and antigen-presenting cell interactions and modulates T-cell responses
    • Katagiri, K., M. Hattori, N. Minato, and T. Kinashi. 2002. Rap1 functions as a key regulator of T-cell and antigen-presenting cell interactions and modulates T-cell responses. Mol. Cell. Biol. 22:1001-1015.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1001-1015
    • Katagiri, K.1    Hattori, M.2    Minato, N.3    Kinashi, T.4
  • 18
    • 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
  • 20
    • 0031472912 scopus 로고    scopus 로고
    • Colocalization of Ras and Ral on the membrane is required for Ras-dependent Ral activation through Ral GDP dissociation stimulator
    • Kishida, S., S. Koyama, K. Matsubara, M. Kishida, Y. Matsuura, and A. Kikuchi. 1997. Colocalization of Ras and Ral on the membrane is required for Ras-dependent Ral activation through Ral GDP dissociation stimulator. Oncogene. 15:2899-2907.
    • (1997) Oncogene , vol.15 , pp. 2899-2907
    • Kishida, S.1    Koyama, S.2    Matsubara, K.3    Kishida, M.4    Matsuura, Y.5    Kikuchi, A.6
  • 21
    • 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
  • 22
    • 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
  • 23
    • 0030766930 scopus 로고    scopus 로고
    • Redistribution and stabilization of cell surface glutamate receptors during synapse formation
    • Mammen, A.L., R.L. Huganir, and R.J. O'Brien. 1997. Redistribution and stabilization of cell surface glutamate receptors during synapse formation. J. Neurosci. 17:7351-7358.
    • (1997) J. Neurosci. , vol.17 , pp. 7351-7358
    • Mammen, A.L.1    Huganir, R.L.2    O'Brien, R.J.3
  • 24
    • 0026744834 scopus 로고
    • Association of rap1 and rap2 proteins with the specific granules of human neutrophils
    • Maridonneau-Parini, I., and J. de Gunzburg. 1992. Association of rap1 and rap2 proteins with the specific granules of human neutrophils. J. Biol. Chem. 267:6396-6402.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6396-6402
    • Maridonneau-Parini, I.1    De Gunzburg, J.2
  • 25
    • 0037044577 scopus 로고    scopus 로고
    • Activation of Gz attenuates Rap1-mediated differentiation of PC12 cells
    • Meng, J., and P.J. Casey. 2002. Activation of Gz attenuates Rap1-mediated differentiation of PC12 cells. J. Biol. Chem. 277:43417-43424.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43417-43424
    • Meng, J.1    Casey, P.J.2
  • 26
    • 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
  • 28
    • 0027176155 scopus 로고
    • Localization of rap1 and rap2 proteins in the gelatinase-containing granules of human neutrophils
    • Mollinedo, F., D. Perez-Sala, C. Gajate, B. Jimenez, P. Rodriguez, and J.C. Lacal. 1993. Localization of rap1 and rap2 proteins in the gelatinase-containing granules of human neutrophils. FEBS Lett. 326:209-214.
    • (1993) FEBS Lett. , vol.326 , pp. 209-214
    • Mollinedo, F.1    Perez-Sala, D.2    Gajate, C.3    Jimenez, B.4    Rodriguez, P.5    Lacal, J.C.6
  • 29
    • 0028990117 scopus 로고
    • A low M(r) GTP-binding protein, Rap1, in human platelets: Localization, translocation and phosphorylation by cyclic AMP-dependent protein kinase
    • Nagata, K., and Y. Nozawa. 1995. A low M(r) GTP-binding protein, Rap1, in human platelets: localization, translocation and phosphorylation by cyclic AMP-dependent protein kinase. Br. J. Haematol. 90:180-186.
    • (1995) Br. J. Haematol. , vol.90 , pp. 180-186
    • Nagata, K.1    Nozawa, Y.2
  • 30
    • 0037450766 scopus 로고    scopus 로고
    • Mechanism of the spatio-temporal regulation of Ras and Rap1
    • Ohba, Y., K. Kurokawa, and M. Matsuda. 2003. Mechanism of the spatio-temporal regulation of Ras and Rap1. EMBO J. 22:859-869.
    • (2003) EMBO J. , vol.22 , pp. 859-869
    • Ohba, Y.1    Kurokawa, K.2    Matsuda, M.3
  • 32
    • 0033180065 scopus 로고    scopus 로고
    • Localization of bud2p, a GTPase-activating protein necessary for programming cell polarity in yeast to the presumptive bud site
    • Park, H.O., A. Sanson, and I. Herskowitz. 1999. Localization of bud2p, a GTPase-activating protein necessary for programming cell polarity in yeast to the presumptive bud site. Genes Dev. 13:1912-1917.
    • (1999) Genes Dev. , vol.13 , pp. 1912-1917
    • Park, H.O.1    Sanson, A.2    Herskowitz, I.3
  • 33
    • 0028246501 scopus 로고
    • Association of Rap1 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 Rap1 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
  • 34
    • 0025961448 scopus 로고
    • Purification of a plasma membrane-associated GTPase-activating protein specific for rap1/Krev-1 from HL60 cells
    • Polakis, P.G., B. Rubinfeld, T. Evans, and F. McCormick. 1991. Purification of a plasma membrane-associated GTPase-activating protein specific for rap1/Krev-1 from HL60 cells. Proc. Natl. Acad. Sci. USA. 88:239-243.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 239-243
    • Polakis, P.G.1    Rubinfeld, B.2    Evans, T.3    McCormick, F.4
  • 35
    • 0033588299 scopus 로고    scopus 로고
    • M-Ras/R-Ras3, a transforming ras protein regulated by Sos1, GRF1, and p120 Ras GTPase-activating protein, interacts with the putative Ras effector AF6
    • Quilliam, L.A., A.F. Castro, K.S. Rogers-Graham, C.B. Martin, C.J. Der, and C. Bi. 1999. M-Ras/R-Ras3, a transforming ras protein regulated by Sos1, GRF1, and p120 Ras GTPase-activating protein, interacts with the putative Ras effector AF6. J. Biol. Chem. 274:23850-23857.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23850-23857
    • Quilliam, L.A.1    Castro, A.F.2    Rogers-Graham, K.S.3    Martin, C.B.4    Der, C.J.5    Bi, C.6
  • 36
    • 0026551586 scopus 로고
    • Subcellular distribution of the Rap1 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 Rap1 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
  • 37
    • 0031569406 scopus 로고    scopus 로고
    • Mutational analysis of the role of Rap1 in regulating cytoskeletal function in Dictyostelium
    • Rebstein, P.J., J. Cardelli, G. Weeks, and G.B. Spiegelman. 1997. Mutational analysis of the role of Rap1 in regulating cytoskeletal function in Dictyostelium. Exp. Cell Res. 231:276-283.
    • (1997) Exp. Cell Res. , vol.231 , pp. 276-283
    • Rebstein, P.J.1    Cardelli, J.2    Weeks, G.3    Spiegelman, G.B.4
  • 38
    • 0032570874 scopus 로고    scopus 로고
    • Costimulation through CD28 suppresses T cell receptor-dependent activation of the Ras-like small GTPase Rap1 in human T lymphocytes
    • Reedquist, K.A., and J.L. Bos. 1998. Costimulation through CD28 suppresses T cell receptor-dependent activation of the Ras-like small GTPase Rap1 in human T lymphocytes. J. Biol. Chem. 273:4944-4949.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4944-4949
    • Reedquist, K.A.1    Bos, J.L.2
  • 40
    • 0028196986 scopus 로고
    • Fluorimetric evaluation of the affinities of isoprenylated peptides for lipid bilayers
    • Silvius, J.R., and F. l'Heureux. 1994. Fluorimetric evaluation of the affinities of isoprenylated peptides for lipid bilayers. Biochemistry. 33:3014-3022.
    • (1994) Biochemistry , vol.33 , pp. 3014-3022
    • Silvius, J.R.1    L'Heureux, F.2
  • 41
    • 0038647351 scopus 로고    scopus 로고
    • The critical cytoplasmic regions of the alphaL/beta2 integrin in Rap1-induced adhesion and migration
    • Tohyama, Y., K. Katagiri, R. Pardi, C. Lu, T. Springer, and T. Kinashi. 2003. The critical cytoplasmic regions of the alphaL/beta2 integrin in Rap1-induced adhesion and migration. Mol. Biol. Cell. 14:2570-2582.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2570-2582
    • Tohyama, Y.1    Katagiri, K.2    Pardi, R.3    Lu, C.4    Springer, T.5    Kinashi, T.6
  • 42
    • 0030963439 scopus 로고    scopus 로고
    • cAMP activates MAP kinase and Elk-1 through a B-Raf- and Rap1-dependent pathway
    • Vossler, M.R., H. Yao, R.D. York, M.G. Pan, C.S. Rim, and P.J. Stork. 1997. cAMP activates MAP kinase and Elk-1 through a B-Raf- and Rap1-dependent pathway. Cell. 89:73-82.
    • (1997) Cell , vol.89 , pp. 73-82
    • Vossler, M.R.1    Yao, H.2    York, R.D.3    Pan, M.G.4    Rim, C.S.5    Stork, P.J.6
  • 44
    • 0037162696 scopus 로고    scopus 로고
    • Ras and Rap control AMPA receptor trafficking during synaptic plasticity
    • Zhu, J., Y. Qin, M. Zhao, L. Van Aelst, and R. Malinow. 2002. Ras and Rap control AMPA receptor trafficking during synaptic plasticity. Cell. 110:443-455.
    • (2002) Cell , vol.110 , pp. 443-455
    • Zhu, J.1    Qin, Y.2    Zhao, M.3    Van Aelst, L.4    Malinow, R.5
  • 45
    • 0032531756 scopus 로고    scopus 로고
    • Extracellular signal-regulated activation of Rap1 fails to interfere in Ras effector signalling
    • Zwartkruis, F.J., R.M. Wolthuis, N.M. Nabben, B. Franke, and J.L. Bos. 1998. Extracellular signal-regulated activation of Rap1 fails to interfere in Ras effector signalling. EMBO J. 17:5905-5912.
    • (1998) EMBO J. , vol.17 , pp. 5905-5912
    • Zwartkruis, F.J.1    Wolthuis, R.M.2    Nabben, N.M.3    Franke, B.4    Bos, J.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.