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Volumn 19, Issue 9, 1999, Pages 6057-6064

The strength of interaction at the Raf cysteine-rich domain is a critical determinant of response of raf to Ras family small GTPases

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATASE; RAF PROTEIN; RAS PROTEIN;

EID: 0032784445     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.19.9.6057     Document Type: Article
Times cited : (73)

References (53)
  • 1
    • 0031919552 scopus 로고    scopus 로고
    • Insulin signal transduction through protein kinase cascades
    • Ayruch, J. 1998. Insulin signal transduction through protein kinase cascades. Mol. Cell. Biochem. 182:31-48.
    • (1998) Mol. Cell. Biochem. , vol.182 , pp. 31-48
    • Ayruch, J.1
  • 2
    • 0030881165 scopus 로고    scopus 로고
    • Mutations of critical amino acids affect the biological and biochemical properties of oncogenic A-Raf and Raf-1
    • Bosch, E., H. Cherwinski, D. Peterson, and M. McMahon. 1997. Mutations of critical amino acids affect the biological and biochemical properties of oncogenic A-Raf and Raf-1. Oncogene 15:1021-1033.
    • (1997) Oncogene , vol.15 , pp. 1021-1033
    • Bosch, E.1    Cherwinski, H.2    Peterson, D.3    McMahon, M.4
  • 5
    • 0027956706 scopus 로고
    • Critical binding and regulatory interactions between Ras and Raf occur through a small, stable N-terminal domain of Raf and specific Ras effector residues
    • Chuang, E., D. Barnard, L. Hettich, X.-F. Zhang, J. Avruch, and M. S. Marshall. 1994. Critical binding and regulatory interactions between Ras and Raf occur through a small, stable N-terminal domain of Raf and specific Ras effector residues. Mol. Cell. Biol. 14:5318-5325.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5318-5325
    • Chuang, E.1    Barnard, D.2    Hettich, L.3    Zhang, X.-F.4    Avruch, J.5    Marshall, M.S.6
  • 7
    • 0027170176 scopus 로고
    • RapV12 antagonizes Ras-dependent activation of ERK1 and ERK2 by LPA and EGF in Rat-1 fibroblast
    • Cook, S. J., B. Rubinfeld, I. Albert, and F. McCormick. 1993. RapV12 antagonizes Ras-dependent activation of ERK1 and ERK2 by LPA and EGF in Rat-1 fibroblast. EMBO J. 12:3475-3485.
    • (1993) EMBO J. , vol.12 , pp. 3475-3485
    • Cook, S.J.1    Rubinfeld, B.2    Albert, I.3    McCormick, F.4
  • 9
    • 0031792782 scopus 로고    scopus 로고
    • The RafC1 cysteine-rich domain contains multiple distinct regulatory epitopes which control Ras-dependent Raf activation
    • Daub, M., J. Jöckel, T. Quack, C. K. Weber, F. Schmitz, U. R. Rapp, A. Wittinghofer, and C. Block. 1998. The RafC1 cysteine-rich domain contains multiple distinct regulatory epitopes which control Ras-dependent Raf activation. Mol. Cell. Biol. 18:6698-6710.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6698-6710
    • Daub, M.1    Jöckel, J.2    Quack, T.3    Weber, C.K.4    Schmitz, F.5    Rapp, U.R.6    Wittinghofer, A.7    Block, C.8
  • 11
    • 0029042701 scopus 로고
    • Regulation of Raf-1 and Raf-1 mutants by Ras-dependent and Ras-independent mechanisms in vitro
    • Dent, P., D. B. Reardon, D. K. Morrison, and T. W. Sturgill. 1995. Regulation of Raf-1 and Raf-1 mutants by Ras-dependent and Ras-independent mechanisms in vitro. Mol. Cell. Biol. 15:4125-4135.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4125-4135
    • Dent, P.1    Reardon, D.B.2    Morrison, D.K.3    Sturgill, T.W.4
  • 13
    • 0028083893 scopus 로고
    • The cysteine-rich region of Raf-1 kinase contains zinc, translocates to liposomes, and is adjacent to a segment that binds GTP-Ras
    • Ghosh, S., W. Q. Xie, A. F. G. Quest, G. M. Mabrouk, J. C. Strum, and R. M. Bell. 1994. The cysteine-rich region of Raf-1 kinase contains zinc, translocates to liposomes, and is adjacent to a segment that binds GTP-Ras. J. Biol. Chem. 269:10000-10007.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10000-10007
    • Ghosh, S.1    Xie, W.Q.2    Quest, A.F.G.3    Mabrouk, G.M.4    Strum, J.C.5    Bell, R.M.6
  • 14
    • 0029913467 scopus 로고    scopus 로고
    • Differential interaction of the Ras family GTP-binding proteins H-Ras, Rap1A, 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, Rap1A, 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
  • 15
    • 0030910890 scopus 로고    scopus 로고
    • Coassociation of Rap1A and Ha-Ras with Raf-1 N-terminal region interferes with Ras-dependent activation of Raf-1
    • Hu, C.-D., K. Kariya, G. Kotani, M. Shirouzu, S. Yokoyama, and T. Kataoka. 1997. Coassociation of Rap1A and Ha-Ras with Raf-1 N-terminal region interferes with Ras-dependent activation of Raf-1. J. Biol. Chem. 272:11702-11705.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11702-11705
    • Hu, C.-D.1    Kariya, K.2    Kotani, G.3    Shirouzu, M.4    Yokoyama, S.5    Kataoka, T.6
  • 16
    • 0032929056 scopus 로고    scopus 로고
    • Effect of phosphorylation on activities of RaplA to interact with Raf-1 and to suppress Ras-dependent Raf-1 activation
    • Hu, C.-D., K. Kariya, T. Okada, X. Qi, C. Song, and T. Kataoka. 1999. Effect of phosphorylation on activities of RaplA to interact with Raf-1 and to suppress Ras-dependent Raf-1 activation. J. Biol. Chem. 274:48-51.
    • (1999) J. Biol. Chem. , vol.274 , pp. 48-51
    • Hu, C.-D.1    Kariya, K.2    Okada, T.3    Qi, X.4    Song, C.5    Kataoka, T.6
  • 17
    • 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
  • 18
    • 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
  • 19
    • 0027500533 scopus 로고
    • The effect of posttranslational modifications on the interaction of Ras2 with adenylyl cyclase
    • Kuroda, Y., N. Suzuki, and T. Kataoka. 1993. The effect of posttranslational modifications on the interaction of Ras2 with adenylyl cyclase. Science 259: 683-686.
    • (1993) Science , vol.259 , pp. 683-686
    • Kuroda, Y.1    Suzuki, N.2    Kataoka, T.3
  • 20
    • 0028272507 scopus 로고
    • Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane
    • Leevers, S. J., H. F. Paterson, and C. J. Marshall. 1994. Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane. Nature 369:411-414.
    • (1994) Nature , vol.369 , pp. 411-414
    • Leevers, S.J.1    Paterson, H.F.2    Marshall, C.J.3
  • 21
    • 0031024585 scopus 로고    scopus 로고
    • An intact Raf zinc finger is required for optimal binding to processed Ras and for Ras-dependent Raf activation in situ
    • Luo, Z., B. Diaz, M. S. Marshall, and J. Avruch. 1997. An intact Raf zinc finger is required for optimal binding to processed Ras and for Ras-dependent Raf activation in situ. Mol. Cell. Biol, 17:46-53.
    • (1997) Mol. Cell. Biol , vol.17 , pp. 46-53
    • Luo, Z.1    Diaz, B.2    Marshall, M.S.3    Avruch, J.4
  • 22
    • 0029006126 scopus 로고
    • Ras recruits Raf-1 to the plasma membrane for activation by tyrosine phosphorylation
    • Marais, R., Y. Light, H. F. Paterson, and C. J. Marshall. 1995. Ras recruits Raf-1 to the plasma membrane for activation by tyrosine phosphorylation. EMBO J. 14:3136-3145.
    • (1995) EMBO J. , vol.14 , pp. 3136-3145
    • Marais, R.1    Light, Y.2    Paterson, H.F.3    Marshall, C.J.4
  • 23
    • 0031041171 scopus 로고    scopus 로고
    • Differential regulation of Raf-1, A-Raf, and B-Raf by oncogenic Ras and tyrosine kinases
    • Marais, R., Y. Light, H. F. Paterson, C. S. Mason, and C. J. Marshall. 1997. Differential regulation of Raf-1, A-Raf, and B-Raf by oncogenic Ras and tyrosine kinases. J. Biol. Chem. 272:4378-4383.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4378-4383
    • Marais, R.1    Light, Y.2    Paterson, H.F.3    Mason, C.S.4    Marshall, C.J.5
  • 24
    • 0029071689 scopus 로고
    • 14-3-3 is not essential for Raf-1 function: Identification of Raf-1 proteins that are biologically activated in a 14-3-3- and Ras-independent manner
    • Michaud, N. R., J. R. Fabian, K. D. Mathes, and D. K. Morrison. 1995. 14-3-3 is not essential for Raf-1 function: identification of Raf-1 proteins that are biologically activated in a 14-3-3- and Ras-independent manner. Mol. Cell. Biol. 15:3390-3397.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3390-3397
    • Michaud, N.R.1    Fabian, J.R.2    Mathes, K.D.3    Morrison, D.K.4
  • 25
    • 0030890762 scopus 로고    scopus 로고
    • Physical association with Ras enhances activation of membrane-bound Raf (RafCAAX)
    • Mineo, C., R. G. W. Anderson, and M. A. White. 1997. Physical association with Ras enhances activation of membrane-bound Raf (RafCAAX). J. Biol. Chem. 272:10345-10348.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10345-10348
    • Mineo, C.1    Anderson, R.G.W.2    White, M.A.3
  • 26
    • 0032575078 scopus 로고    scopus 로고
    • Isolation of a new protein factor required for activation of Raf-1 by Ha-Ras: Partial purification from rat brain cytosols
    • Mizutani, S., H. Koide, and Y. Kaziro. 1998. Isolation of a new protein factor required for activation of Raf-1 by Ha-Ras: partial purification from rat brain cytosols. Oncogene 16:2781-2786.
    • (1998) Oncogene , vol.16 , pp. 2781-2786
    • Mizutani, S.1    Koide, H.2    Kaziro, Y.3
  • 28
    • 0029757119 scopus 로고    scopus 로고
    • The solution structure of the Raf-1 cysteine-rich domain: A novel Ras and phospholipid binding site
    • Mott, H. R., J. W. Carpenter, S. Zhong, S. Ghosh, R. M. Bell, and S. L. Campbell. 1996. The solution structure of the Raf-1 cysteine-rich domain: a novel Ras and phospholipid binding site. Proc. Natl. Acad. Sci. USA 93: 8312-8317.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8312-8317
    • Mott, H.R.1    Carpenter, J.W.2    Zhong, S.3    Ghosh, S.4    Bell, R.M.5    Campbell, S.L.6
  • 30
    • 0029107760 scopus 로고
    • The 2,2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rapla and a GTP analogue
    • Nassar, N., G. Horn, C. Herrmann, A. Scherer, F. McCormick, and A. Wittinghofer. 1995. The 2,2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with RaplA and a GTP analogue. Nature 375:554-560.
    • (1995) Nature , vol.375 , pp. 554-560
    • Nassar, N.1    Horn, G.2    Herrmann, C.3    Scherer, A.4    McCormick, F.5    Wittinghofer, A.6
  • 31
    • 0030048696 scopus 로고    scopus 로고
    • Activation of brain B-Raf protein kinase by Rap1B small GTP-binding protein
    • Ohtsuka, T., K. Shimizu, B. Yamamori, S. Kuroda, and Y. Takai. 1996. Activation of brain B-Raf protein kinase by Rap1B small GTP-binding protein. J. Biol. Chem. 271:1258-1261.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1258-1261
    • Ohtsuka, T.1    Shimizu, K.2    Yamamori, B.3    Kuroda, S.4    Takai, Y.5
  • 32
    • 0029919472 scopus 로고    scopus 로고
    • Post-translational modification of H-Ras is required for activation of, but not for association with, B-Raf
    • Okada, T., T. Masuda, M. Shinkai, K. Kariya, and T. Kataoka. 1996. Post-translational modification of H-Ras is required for activation of, but not for association with, B-Raf. J. Biol. Chem. 271:4671-4678.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4671-4678
    • Okada, T.1    Masuda, T.2    Shinkai, M.3    Kariya, K.4    Kataoka, T.5
  • 33
    • 0032544525 scopus 로고    scopus 로고
    • Modulation of kinase activity and oncogenic properties by alternative splicing reveals a novel regulatory mechanism for B-Raf
    • Papin, C., A. Denouel-Galy, D. Laugler, G. Calothy, and A. Eychène. 1998. Modulation of kinase activity and oncogenic properties by alternative splicing reveals a novel regulatory mechanism for B-Raf. J. Biol. Chem. 273: 24939-24947.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24939-24947
    • Papin, C.1    Denouel-Galy, A.2    Laugler, D.3    Calothy, G.4    Eychène, A.5
  • 34
    • 0023721977 scopus 로고
    • Human cDNAs rap 1 and rap 2 homologous to the Drosophila gene Dras 3 encode proteins closely related to ras in the "effector" region
    • Pizon, V., P. Chardin, I. Lerosey, B. Olofsson, and A. Tavitian. 1988. Human cDNAs rap 1 and rap 2 homologous to the Drosophila gene Dras 3 encode proteins closely related to ras in the "effector" region. Oncogene 3:201-204.
    • (1988) Oncogene , vol.3 , pp. 201-204
    • Pizon, V.1    Chardin, P.2    Lerosey, I.3    Olofsson, B.4    Tavitian, A.5
  • 36
    • 0030854042 scopus 로고    scopus 로고
    • Activity of plasma membrane-recruited Raf-1 is regulated by Ras via the Raf zinc finger
    • Roy, S., A. Lane, J. Yan, R. McPherson, and J. F. Hancock. 1997. Activity of plasma membrane-recruited Raf-1 is regulated by Ras via the Raf zinc finger. J. Biol. Chem. 272:20139-20145.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20139-20145
    • Roy, S.1    Lane, A.2    Yan, J.3    McPherson, R.4    Hancock, J.F.5
  • 39
    • 0025604178 scopus 로고
    • Complete coding sequence of a human B-raf cDNA and detection of B-raf protein kinase with isozyme specific antibodies
    • Sithanandam, G., W. Kolch, F.-M. Duh, and U. R. Rapp. 1990. Complete coding sequence of a human B-raf cDNA and detection of B-raf protein kinase with isozyme specific antibodies. Oncogene 5:1775-1780.
    • (1990) Oncogene , vol.5 , pp. 1775-1780
    • Sithanandam, G.1    Kolch, W.2    Duh, F.-M.3    Rapp, U.R.4
  • 40
    • 0028241533 scopus 로고
    • Activation of Raf as a result of recruitment to the plasma membrane
    • Stokoe, D., S. G. Macdonald, K. Cadwallander, M. Symons, and J. F. Hancock. 1994. Activation of Raf as a result of recruitment to the plasma membrane. Science 264:1463-1467.
    • (1994) Science , vol.264 , pp. 1463-1467
    • Stokoe, D.1    Macdonald, S.G.2    Cadwallander, K.3    Symons, M.4    Hancock, J.F.5
  • 41
    • 0030919893 scopus 로고    scopus 로고
    • Activation of c-Raf-1 by Ras and Src through different mechanisms: Activation in vivo and in vitro
    • Stokoe, D., and F. McCormick. 1997. Activation of c-Raf-1 by Ras and Src through different mechanisms: activation in vivo and in vitro. EMBO J. 16:2384-2396.
    • (1997) EMBO J. , vol.16 , pp. 2384-2396
    • Stokoe, D.1    McCormick, F.2
  • 42
    • 0025266334 scopus 로고
    • Expression of raf family proto-oncogenes in normal mouse tissues
    • Storm, S. M., J. L. Cleveland, and U. R. Rapp. 1990. Expression of raf family proto-oncogenes in normal mouse tissues. Oncogene 5:345-351.
    • (1990) Oncogene , vol.5 , pp. 345-351
    • Storm, S.M.1    Cleveland, J.L.2    Rapp, U.R.3
  • 43
    • 0031458739 scopus 로고    scopus 로고
    • Membrane recruitment of Raf-1 is not the only function of Ras in Raf-1 activation
    • Tamada, M., C.-D. Hu, K. Kariya, T. Okada, and T. Kataoka. 1997. Membrane recruitment of Raf-1 is not the only function of Ras in Raf-1 activation. Oncogene 15:2959-2964.
    • (1997) Oncogene , vol.15 , pp. 2959-2964
    • Tamada, M.1    Hu, C.-D.2    Kariya, K.3    Okada, T.4    Kataoka, T.5
  • 45
    • 0032474838 scopus 로고    scopus 로고
    • A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity
    • Tzivion, G., Z. Luo, and J. Avruch. 1998. A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity. Nature 394:88-92.
    • (1998) Nature , vol.394 , pp. 88-92
    • Tzivion, G.1    Luo, Z.2    Avruch, J.3
  • 46
    • 0027250250 scopus 로고
    • Mammalian Ras interacts directly with the serine/threonine kinase Raf
    • Vojtek, A. B., S. M. Hollenberg, and J. A. Cooper. 1993. Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell 74:205-214.
    • (1993) Cell , vol.74 , pp. 205-214
    • Vojtek, A.B.1    Hollenberg, S.M.2    Cooper, J.A.3
  • 47
    • 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. S. 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.S.6
  • 48
    • 0032555494 scopus 로고    scopus 로고
    • Identification of residues in the cysteine-rich domain of Raf-1 that control Ras binding and Raf-1 activity
    • Winkler, D. G., R. E. Cutler, Jr., J. K. Drugan, S. Campbell, D. K. Morrison, and A. J. Cooper. 1998. Identification of residues in the cysteine-rich domain of Raf-1 that control Ras binding and Raf-1 activity. J. Biol. Chem. 273: 21578-21584.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21578-21584
    • Winkler, D.G.1    Cutler R.E., Jr.2    Drugan, J.K.3    Campbell, S.4    Morrison, D.K.5    Cooper, A.J.6
  • 49
    • 0030464444 scopus 로고    scopus 로고
    • How Ras-related proteins talk to their effectors
    • Wittinghofer, A., and N. Nassar. 1996. How Ras-related proteins talk to their effectors. Trends Biochem. Sci. 21:488-491.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 488-491
    • Wittinghofer, A.1    Nassar, N.2
  • 50
    • 0029058730 scopus 로고
    • Purification of a Ras-dependent mitogen-activated protein kinase kinase kinase from bovine brain cytosol and its identification as a complex of B-Raf and 14-3-3 proteins
    • Yamamori, B., S. Kuroda, K. Shimizu, K. Fukui, T. Ohtsuka, and Y. Takai. 1995. Purification of a Ras-dependent mitogen-activated protein kinase kinase kinase from bovine brain cytosol and its identification as a complex of B-Raf and 14-3-3 proteins. J. Biol. Chem. 270:11723-11726.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11723-11726
    • Yamamori, B.1    Kuroda, S.2    Shimizu, K.3    Fukui, K.4    Ohtsuka, T.5    Takai, Y.6
  • 53
    • 0025988826 scopus 로고
    • Random mutagenesis of gene-sized DNA molecules by use of PCR with Taq DNA polymerase
    • Zhou, Y., X. Zhang, and R. H. Ebright. 1991. Random mutagenesis of gene-sized DNA molecules by use of PCR with Taq DNA polymerase. Nucleic Acids Res. 19:6052.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 6052
    • Zhou, Y.1    Zhang, X.2    Ebright, R.H.3


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