메뉴 건너뛰기




Volumn 396, Issue 6707, 1998, Pages 180-183

The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR; GUANINE NUCLEOTIDE EXCHANGE FACTOR; PHOSPHATIDYLINOSITOL 3 HYDROXYKINASE; PROTEIN P21; RAF PROTEIN; RAS PROTEIN; SERINE; UNCLASSIFIED DRUG;

EID: 0032511882     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/24184     Document Type: Article
Times cited : (389)

References (22)
  • 3
    • 0028073606 scopus 로고
    • Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation
    • Freed, E., Symons, M., Macdonald, S. G., McCormick, F. & Ruggieri, R. Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation. Science 265, 1713-1716 (1994).
    • (1994) Science , vol.265 , pp. 1713-1716
    • Freed, E.1    Symons, M.2    Macdonald, S.G.3    McCormick, F.4    Ruggieri, R.5
  • 4
    • 0029014973 scopus 로고
    • Reversal of Raf-1 activation by purified and membrane-associated protein phosphatases
    • Dent, P., Jelinek, T., Morrison, D. K., Weber, M. J. & Sturgill, T. W. Reversal of Raf-1 activation by purified and membrane-associated protein phosphatases. Science 268, 1902-1906 (1995).
    • (1995) Science , vol.268 , pp. 1902-1906
    • Dent, P.1    Jelinek, T.2    Morrison, D.K.3    Weber, M.J.4    Sturgill, T.W.5
  • 5
    • 0028846902 scopus 로고
    • Mechanisms regulating Raf-1 activity in signal transduction pathways
    • Morrison, D. K. Mechanisms regulating Raf-1 activity in signal transduction pathways. Mol. Reprod. Dev. 42, 507-514 (1995).
    • (1995) Mol. Reprod. Dev. , vol.42 , pp. 507-514
    • Morrison, D.K.1
  • 6
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • Muslin, A. J., Tanner, J. W., Allen, P. M. & Shaw, A. S. Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 84, 889-897 (1996).
    • (1996) Cell , vol.84 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 8
    • 0029006126 scopus 로고
    • Ras recruits Raf-1 to the plasma membrane for activation by tyrosine phosphorylation
    • Marais, R., Light, Y., Paterson, H. F. & Marshall, C. J. Ras recruits Raf-1 to the plasma membrane for activation by tyrosine phosphorylation. EMBO J. 14, 3136-3145 (1995).
    • (1995) EMBO J. , vol.14 , pp. 3136-3145
    • Marais, R.1    Light, Y.2    Paterson, H.F.3    Marshall, C.J.4
  • 9
    • 0030756069 scopus 로고    scopus 로고
    • Phosphorylation of Raf-1 serine 338-serine 339 is an essential regulatory event for Ras-dependent activation and biological signaling
    • Diaz, B. et al. Phosphorylation of Raf-1 serine 338-serine 339 is an essential regulatory event for Ras-dependent activation and biological signaling. Mol. Cell. Biol. 17, 4509-4516 (1997).
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4509-4516
    • Diaz, B.1
  • 10
    • 85046500990 scopus 로고    scopus 로고
    • Oncogenes, growth factors and phorbol esters regulate Raf-1 through common mechanisms
    • in the press
    • Barnard, D., Diaz, B., Clawson, D. & Marshall, M. Oncogenes, growth factors and phorbol esters regulate Raf-1 through common mechanisms. Oncogene (in the press).
    • Oncogene
    • Barnard, D.1    Diaz, B.2    Clawson, D.3    Marshall, M.4
  • 11
    • 0028078824 scopus 로고
    • A brain serine/threonine protein kinase activated by Cdc42 and Rac1
    • Manser, E., Leung, T., Salihuddin, H., Zhao, Z.-S. & Lim, L. A brain serine/threonine protein kinase activated by Cdc42 and Rac1. Nature 367, 40-46 (1994).
    • (1994) Nature , vol.367 , pp. 40-46
    • Manser, E.1    Leung, T.2    Salihuddin, H.3    Zhao, Z.-S.4    Lim, L.5
  • 12
    • 0032559211 scopus 로고    scopus 로고
    • Coupling of Ras and Rac guanosine triphosphatases through the Ras exchanger Sos
    • Nimnual, A. S., Yatsula, B. A. & Bar-Sagi, D. Coupling of Ras and Rac guanosine triphosphatases through the Ras exchanger Sos. Science 279, 560-563 (1998).
    • (1998) Science , vol.279 , pp. 560-563
    • Nimnual, A.S.1    Yatsula, B.A.2    Bar-Sagi, D.3
  • 13
    • 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. et al. Role of substrates and products of PI 3-kinase in regulating activation of Rac related guanosine triphosphatases by Vav. Science 279, 558-560 (1998).
    • (1998) Science , vol.279 , pp. 558-560
    • Han, J.1
  • 14
    • 0030811528 scopus 로고    scopus 로고
    • Kinase-deficient Pak1 mutants inhibit Ras transformation of Rat-1 fibroblasts
    • Tang, Y. et al. Kinase-deficient Pak1 mutants inhibit Ras transformation of Rat-1 fibroblasts. Mol. Cell. Biol. 17, 4454-4464 (1997).
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4454-4464
    • Tang, Y.1
  • 15
    • 0029829898 scopus 로고    scopus 로고
    • Cleavage arrest of early frog embryos by the G protein-activated protein kinase PakI
    • Rooney, R. D. et al. Cleavage arrest of early frog embryos by the G protein-activated protein kinase PakI. J. Biol. Chem. 271, 21498-21504 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 21498-21504
    • Rooney, R.D.1
  • 16
    • 0030918572 scopus 로고    scopus 로고
    • Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2
    • Rudel, T. & Bokoch, G. M. Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2. Science 276, 1571-1574 (1997).
    • (1997) Science , vol.276 , pp. 1571-1574
    • Rudel, T.1    Bokoch, G.M.2
  • 17
    • 0030830220 scopus 로고    scopus 로고
    • Cross-cascade activation of ERKs and ternary complex factors by Rho family proteins
    • Frost, J. A. et al. Cross-cascade activation of ERKs and ternary complex factors by Rho family proteins. EMBO J. 16, 6426-6438 (1997).
    • (1997) EMBO J. , vol.16 , pp. 6426-6438
    • Frost, J.A.1
  • 18
    • 0020364214 scopus 로고
    • Experimentally improved reliability of ultrasensitive silver staining of protein in polyacrylamide gels
    • Eschenbruch, M. & Bürk, R. R. Experimentally improved reliability of ultrasensitive silver staining of protein in polyacrylamide gels. Anal. Biochem. 125, 96-99 (1982).
    • (1982) Anal. Biochem. , vol.125 , pp. 96-99
    • Eschenbruch, M.1    Bürk, R.R.2
  • 20
    • 0028239183 scopus 로고
    • Differential Raf requirement for activation of mitogen-activated protein kinase by growth factors, phorbol esters, and calcium
    • Chao, T.-S. O., Foster, D. A., Rapp, U. R. & Rosner, M. R. Differential Raf requirement for activation of mitogen-activated protein kinase by growth factors, phorbol esters, and calcium. J. Biol. Chem. 269, 7337-7341 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 7337-7341
    • Chao, T.-S.O.1    Foster, D.A.2    Rapp, U.R.3    Rosner, M.R.4
  • 21
    • 0025998840 scopus 로고
    • Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates
    • Boyle, W. J., van der Geer, P. & Hunter, T. Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates. Methods Enzymol. 201, 110-149 (1991).
    • (1991) Methods Enzymol. , vol.201 , pp. 110-149
    • Boyle, W.J.1    Van Der Geer, P.2    Hunter, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.