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Volumn 30, Issue 19, 2010, Pages 4698-4711

Impaired binding of 14-3-3 to C-RAF in Noonan syndrome suggests new approaches in diseases with increased ras signaling

Author keywords

[No Author keywords available]

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN 14 3 3; RAF PROTEIN; RAS PROTEIN;

EID: 77956687588     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.01636-09     Document Type: Article
Times cited : (100)

References (56)
  • 1
    • 33646926129 scopus 로고    scopus 로고
    • 14-3-3 proteins: A historic overview
    • Aitken, A. 2006. 14-3-3 proteins: a historic overview. Semin. Cancer Biol. 16:162-172.
    • (2006) Semin. Cancer Biol. , vol.16 , pp. 162-172
    • Aitken, A.1
  • 2
  • 3
    • 0029879058 scopus 로고    scopus 로고
    • Quantitative structure-activity analysis correlating Ras/Raf interaction in vitro to Raf activation in vivo
    • Block, C., R. Janknecht, C. Herrmann, N. Nassar, and A. Wittinghofer. 1996. Quantitative structure-activity analysis correlating Ras/Raf interaction in vitro to Raf activation in vivo. Nat. Struct. Biol. 3:244-251.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 244-251
    • Block, C.1    Janknecht, R.2    Herrmann, C.3    Nassar, N.4    Wittinghofer, A.5
  • 6
    • 69249216345 scopus 로고    scopus 로고
    • The C-terminus of Raf-1 acts as a 14-3-3-dependent activation switch
    • Dhillon, A. S., Y. Y. Yip, G. J. Grindlay, J. L. Pakay, and M. Dangers. 2009. The C-terminus of Raf-1 acts as a 14-3-3-dependent activation switch. Cell. Signal. 21:1645-1651.
    • (2009) Cell. Signal. , vol.21 , pp. 1645-1651
    • Dhillon, A.S.1    Yip, Y.Y.2    Grindlay, G.J.3    Pakay, J.L.4    Dangers, M.5
  • 7
    • 0037264633 scopus 로고    scopus 로고
    • Targeting RAS signalling pathways in cancer therapy
    • Downward, F. 2003. Targeting RAS signalling pathways in cancer therapy. Nat. Rev. Cancer 3:11-22.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 11-22
    • Downward, F.1
  • 8
    • 0041529686 scopus 로고    scopus 로고
    • Protein kinase a blocks Raf-1 activity by stimulating 14-3-3 binding and blocking Raf-1 interaction with Ras
    • Dumaz, N., and R. Marais. 2003. Protein kinase A blocks Raf-1 activity by stimulating 14-3-3 binding and blocking Raf-1 interaction with Ras. J. Biol. Chem. 278:29819-29823.
    • (2003) J. Biol. Chem. , vol.278 , pp. 29819-29823
    • Dumaz, N.1    Marais, R.2
  • 9
    • 14044252680 scopus 로고    scopus 로고
    • Interaction of 14-3-3 protein with Chk1 affects localization and checkpoint function
    • Dunaway, S., H. Y. Liu, and N. C. Walworth. 2005. Interaction of 14-3-3 protein with Chk1 affects localization and checkpoint function. J. Cell Sci. 118:39-50.
    • (2005) J. Cell Sci. , vol.118 , pp. 39-50
    • Dunaway, S.1    Liu, H.Y.2    Walworth, N.C.3
  • 10
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics. Acta Crystallogr
    • Emsley, P., and K. Cowtan. 2004. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60:2126-2132.
    • (2004) D Biol. Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 11
    • 27544453376 scopus 로고    scopus 로고
    • Mutations of C-RAF are rare in human cancer because C-RAF has a low basal kinase activity compared with B-RAF
    • DOI 10.1158/0008-5472.CAN-05-1683
    • Emuss, V., M. Garnett, C. Mason, and R. Marais. 2005. Mutations of C-RAF are rare in human cancer because C-RAF has a low basal kinase activity compared with B-RAF. Cancer Res. 65:9719-9726. (Pubitemid 41541448)
    • (2005) Cancer Research , vol.65 , Issue.21 , pp. 9719-9726
    • Emuss, V.1    Garnett, M.2    Mason, C.3    Marais, R.4
  • 14
    • 0028073606 scopus 로고
    • Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation
    • Freed, E., M. Symons, S. G Macdonald, F. McCormick, and R. Ruggieri. 1994. Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation. Science 265:1713-1716. (Pubitemid 24314903)
    • (1994) Science , vol.265 , Issue.5179 , pp. 1713-1716
    • Freed, E.1    Symons, M.2    Macdonald, S.G.3    McCormick, F.4    Ruggieri, R.5
  • 15
    • 0027461546 scopus 로고
    • The eukaryotic host factor that activates exoenzyme S of Pseudomonas aeruginosa is a member of the 14-3-3 protein family
    • Fu, H., J. Coburn, and R. J. Collier. 1993. The eukaryotic host factor that activates exoenzyme S of Pseudomonas aeruginosa is a member of the 14-3-3 protein family. Proc. Natl. Acad. Sci. U. S. A. 90:2320-2324.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 2320-2324
    • Fu, H.1    Coburn, J.2    Collier, R.J.3
  • 17
    • 1842740348 scopus 로고    scopus 로고
    • Dynamic changes in C-Raf phosphorylation and 14-3-3 protein binding in response to growth factor stimulation: Differential roles of 14-3-3 protein binding sites
    • Hekman, M., S. Wiese, R. Metz, S. Albert, J. Troppmair, J. Nickel, M. Sendtner, and U. R. Rapp. 2004. Dynamic changes in C-Raf phosphorylation and 14-3-3 protein binding in response to growth factor stimulation: differential roles of 14-3-3 protein binding sites. J. Biol. Chem. 279:14074-14086.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14074-14086
    • Hekman, M.1    Wiese, S.2    Metz, R.3    Albert, S.4    Troppmair, J.5    Nickel, J.6    Sendtner, M.7    Rapp, U.R.8
  • 18
    • 0345059753 scopus 로고    scopus 로고
    • The 14-3-3 cancer connection
    • Hermeking, H. 2003. The 14-3-3 cancer connection. Nat. Rev. Cancer 3:931-943.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 931-943
    • Hermeking, H.1
  • 19
    • 33744544172 scopus 로고    scopus 로고
    • 14-3-3 proteins in cell cycle regulation
    • Hermeking, H., and A. Benzinger. 2006. 14-3-3 proteins in cell cycle regulation. Semin. Cancer Biol. 16:183-192.
    • (2006) Semin. Cancer Biol. , vol.16 , pp. 183-192
    • Hermeking, H.1    Benzinger, A.2
  • 21
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. 1993. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26:795-800.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 22
    • 70350452750 scopus 로고    scopus 로고
    • Cell type-specific importance of Ras-c-Raf complex association rate constants for MAPK signalling
    • Kiel, C., and L. Serrano. 2009. Cell type-specific importance of Ras-c-Raf complex association rate constants for MAPK signalling. Sci. Signal. 2:ra38.
    • (2009) Sci. Signal. , vol.2
    • Kiel, C.1    Serrano, L.2
  • 23
    • 0036297889 scopus 로고    scopus 로고
    • 14-3-3 antagonizes Ras-mediated Raf-1 recruitment to the plasma membrane to maintain signaling fidelity
    • Light, Y., H. Paterson, and R. Marais. 2002. 14-3-3 antagonizes Ras-mediated Raf-1 recruitment to the plasma membrane to maintain signaling fidelity. Mol. Cell. Biol. 22:4984-4996.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4984-4996
    • Light, Y.1    Paterson, H.2    Marais, R.3
  • 24
    • 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
  • 25
    • 0035930343 scopus 로고    scopus 로고
    • C-TAK1 Regulates Ras Signaling by Phosphorylating the MAPK Scaffold, KSR1
    • DOI 10.1016/S1097-2765(01)00383-5
    • Müller, J., S. Ory, T. Copeland, H. Piwnica-Worms, and D. K. Morrison. 2001. C-TAK1 regulates Ras signaling by phosphorylating the MAPK scaffold, KSR1. Mol. Cell 8:983-993. (Pubitemid 34031801)
    • (2001) Molecular Cell , vol.8 , Issue.5 , pp. 983-993
    • Muller, J.1    Ory, S.2    Copeland, T.3    Piwnica-Worms, H.4    Morrison, D.K.5
  • 27
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signalling proteins is mediated by the recognition of phosphoserine
    • Muslin, A. J., J. W. Tanner, P. M. Allen, and A. S. Shaw. 1996. Interaction of 14-3-3 with signalling proteins is mediated by the recognition of phosphoserine. Cell 84:889-897.
    • (1996) Cell , vol.84 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 28
    • 33646757492 scopus 로고    scopus 로고
    • On the nature of cavities on protein surfaces: Application to the identification of drug-binding sites
    • DOI 10.1002/prot.20897
    • Nayal, M., and B. Honig. 2006. On the nature of cavities on protein surfaces: application to the identification of drug-binding sites. Proteins 63:892-906. (Pubitemid 43765141)
    • (2006) Proteins: Structure, Function and Genetics , vol.63 , Issue.4 , pp. 892-906
    • Nayal, M.1    Honig, B.2
  • 29
    • 0035917466 scopus 로고    scopus 로고
    • Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. A role for scaffolding in enzyme regulation
    • Obsil, T., R. Ghirlando, D. C. Klein, S. Ganguly, and F. Dyda. 2001. Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. A role for scaffolding in enzyme regulation. Cell 105:257-267.
    • (2001) Cell , vol.105 , pp. 257-267
    • Obsil, T.1    Ghirlando, R.2    Klein, D.C.3    Ganguly, S.4    Dyda, F.5
  • 30
    • 0030879911 scopus 로고    scopus 로고
    • Topology and target interaction of the fusicoccin-binding 14-3-3 homologs of Commelina communis
    • DOI 10.1046/j.1365-313X.1997.12020441.x
    • Oecking, C., M. Piotrowski, J. Hagemeier, and K. Hagemann. 1997. Topology and target interaction of the fusicoccin-binding 14-3-3 homologs of Commelina communis. Plant J. 12:441-453. (Pubitemid 27389631)
    • (1997) Plant Journal , vol.12 , Issue.2 , pp. 441-453
    • Oecking, C.1    Piotrowski, M.2    Hagemeier, J.3    Hagemann, K.4
  • 33
    • 60149087610 scopus 로고    scopus 로고
    • A structural rationale for selective stabilization of antitumor interactions of 14-3-3 proteins by cotylenin A
    • Ottmann, C., M. Weyand, T. Sassa, T. Inoue, N. Kato, A. Wittinghofer, and C. Oecking. 2009. A structural rationale for selective stabilization of antitumor interactions of 14-3-3 proteins by cotylenin A. J. Mol. Biol. 386:913-919.
    • (2009) J. Mol. Biol. , vol.386 , pp. 913-919
    • Ottmann, C.1    Weyand, M.2    Sassa, T.3    Inoue, T.4    Kato, N.5    Wittinghofer, A.6    Oecking, C.7
  • 36
    • 0032568665 scopus 로고    scopus 로고
    • 14-3-3ζ binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove
    • Petosa, C., S. C. Masters, L. A. Bankston, J. Pohl, B. Wang, H. Fu, and R. C. Liddington. 1998. 14-3-3ζ binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove. J. Biol. Chem. 273:16305-16310.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16305-16310
    • Petosa, C.1    Masters, S.C.2    Bankston, L.A.3    Pohl, J.4    Wang, B.5    Fu, H.6    Liddington, R.C.7
  • 37
    • 77950361185 scopus 로고    scopus 로고
    • Mechanistic differences in the transcriptional activation of p53 by 14-3-3 isoforms
    • Rajagopalan, S., R. S. Sade, F. M. Townsley, and A. R. Fersht. 2010. Mechanistic differences in the transcriptional activation of p53 by 14-3-3 isoforms. Nucleic Acids Res. 38:893-906.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 893-906
    • Rajagopalan, S.1    Sade, R.S.2    Townsley, F.M.3    Fersht, A.R.4
  • 39
    • 0033180582 scopus 로고    scopus 로고
    • Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding
    • Rittinger, K., J. Budman, J. Xu, S. Volinia, L. C. Cantley, S. J. Smerdon, S. J. Gamblin, and M. B. Yaffe. 1999. Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding. Mol. Cell 4:153-166.
    • (1999) Mol. Cell , vol.4 , pp. 153-166
    • Rittinger, K.1    Budman, J.2    Xu, J.3    Volinia, S.4    Cantley, L.C.5    Smerdon, S.J.6    Gamblin, S.J.7    Yaffe, M.B.8
  • 44
    • 33947594129 scopus 로고    scopus 로고
    • Hyperactive Ras in developmental disorders and cancer
    • Schubbert, S., K. Shannon, and G. Bollag. 2007. Hyperactive Ras in developmental disorders and cancer. Nat. Rev. Cancer 7:295-308.
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 295-308
    • Schubbert, S.1    Shannon, K.2    Bollag, G.3
  • 46
    • 77951296388 scopus 로고    scopus 로고
    • Structure of the p53 C-terminus bound to 14-3-3: Implications for stabilization of the p53 tetramer
    • Schumacher, B., J. Mondry, P. Thiel, M. Weyand, and C. Ottmann. 2010. Structure of the p53 C-terminus bound to 14-3-3: implications for stabilization of the p53 tetramer. FEBS Lett. 584:1443-1448.
    • (2010) FEBS Lett. , vol.584 , pp. 1443-1448
    • Schumacher, B.1    Mondry, J.2    Thiel, P.3    Weyand, M.4    Ottmann, C.5
  • 47
    • 0028241533 scopus 로고
    • Activation of Raf as a result of recruitment to the plasma membrane
    • Stokoe, D., S. G. Macdonald, K. Cadwallader, M. Symons, and F. Hancock. 1994. Activation of Raf as a result of recruitment to the plasma membrane. Science 264:1463-1467. (Pubitemid 24217138)
    • (1994) Science , vol.264 , Issue.5164 , pp. 1463-1467
    • Stokoe, D.1    Macdonald, S.G.2    Cadwallader, K.3    Symons, M.4    Hancock, J.F.5
  • 50
    • 0032474838 scopus 로고    scopus 로고
    • A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity
    • Tzivion, G., Z. Lou, and J. Avruch. 1998. A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity. Nature 394:536-539.
    • (1998) Nature , vol.394 , pp. 536-539
    • Tzivion, G.1    Lou, Z.2    Avruch, J.3
  • 53
    • 0037416221 scopus 로고    scopus 로고
    • Structural view of a fungal toxin acting on a 14-3-3 regulatory complex
    • DOI 10.1093/emboj/cdg104
    • Würtele, M., C. Jelich-Ottmann, A. Wittinghofer, and C. Oecking. 2003. Structural view of a fungal toxin acting on a 14-3-3 regulatory complex. EMBO J. 22:987-994. (Pubitemid 36313583)
    • (2003) EMBO Journal , vol.22 , Issue.5 , pp. 987-994
    • Wurtele, M.1    Jelich-Ottmann, C.2    Wittinghofer, A.3    Oecking, C.4
  • 54
    • 0037138389 scopus 로고    scopus 로고
    • How do 14-3-3 proteins work? - Gatekeeper phosphorylation and the molecular anvil hypothesis
    • Yaffe, M. B. 2002. How do 14-3-3 proteins work? - Gatekeeper phosphorylation and the molecular anvil hypothesis. FEBS Lett. 513:53-57.
    • (2002) FEBS Lett. , vol.513 , pp. 53-57
    • Yaffe, M.B.1
  • 56
    • 14744301343 scopus 로고    scopus 로고
    • JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of c-Abl in the apoptotic response to DNA damage
    • Yoshida, K., T. Yamaguchi, T. Natsume, D. Kufe, and Y. Miki. 2005. JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of c-Abl in the apoptotic response to DNA damage. Nat. Cell Biol. 7:278-285
    • (2005) Nat. Cell Biol. , vol.7 , pp. 278-285
    • Yoshida, K.1    Yamaguchi, T.2    Natsume, T.3    Kufe, D.4    Miki, Y.5


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