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Volumn 9, Issue 2, 1997, Pages 174-179

The complexity of Raf-1 regulation

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN SERINE THREONINE KINASE; RAF PROTEIN; RAS PROTEIN;

EID: 0030898415     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(97)80060-9     Document Type: Article
Times cited : (544)

References (62)
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    • Mammalian p50 Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4
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    • Stepanova L, Leng X, Parker SB, Harper JW: Mammalian p50 Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4. Genes Dev 1996, 10:1491-1502. p50 is identified as the mammalian homolog of cdc37 from Saccharomyces cerevisiae and is reported to be the protein kinase targeting subunit of the molecular chaperone hsp90.
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    • Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association
    • See annotation [43•]
    • Schulte TW, Blagosklonny MV, Ingui C, Neckers L: Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association. J Biol Chem 1995, 270:24585-24588. See annotation [43•].
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    • Destabilization of Raf-1 by geldanamycin leads to disruption of the Raf-1-MEK-mitogen-activated protein kinase signalling pathway
    • These papers [42•,43•] show that pharmacological disruption of the Raf-1-hsp90 complex destabilizes the endogenous Raf-1 protein and disrupts Raf-1-mediated signal transduction
    • Schulte TW, Blagosklonny MV, Romanova L, Mushinski JF, Monia BP, Johnston JF, Nguyen P, Trepel J, Neckers LM: Destabilization of Raf-1 by geldanamycin leads to disruption of the Raf-1-MEK-mitogen-activated protein kinase signalling pathway. Mol Cell Biol 1996, 16:5839-5845. These papers [42•,43•] show that pharmacological disruption of the Raf-1-hsp90 complex destabilizes the endogenous Raf-1 protein and disrupts Raf-1-mediated signal transduction.
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    • KSR modulates signal propagation within the MAPK cascade
    • This paper examines the function of the mammalian homolog of the Drosophila and Caenorhabditis elegans protein KSR, and finds that KSR facilitates signal transduction between Raf-1, MEK, and MAPK. KSR is also shown to associate with Raf-1 at the membrane in a Ras-dependent manner, indicating the presence of a membrane-bound signaling complex
    • Therrien M, Michaud NR, Rubin GM, Morrison DK: KSR modulates signal propagation within the MAPK cascade. Genes Dev 1996, 10:2684-2695. This paper examines the function of the mammalian homolog of the Drosophila and Caenorhabditis elegans protein KSR, and finds that KSR facilitates signal transduction between Raf-1, MEK, and MAPK. KSR is also shown to associate with Raf-1 at the membrane in a Ras-dependent manner, indicating the presence of a membrane-bound signaling complex.
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    • Activation of the Raf-1 kinase cascade by coumermycin-induced dimerization
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    • These two papers [45•,46•] show that Raf-1 can be activated by chemical-induced oligomerization. However, while Farrar et al. [45•] found that the activation of Raf-1 by oligomerization is Ras-independent, Luo et al. [46•] found that an interaction with Ras is required
    • Luo Z, Tzivion G, Belshaw PJ, Vawas D, Marshall M, Avruch J: Oligomerization activates c-Raf-1 through a Ras-dependent mechanism. Nature 1996, 383:181-185. These two papers [45•,46•] show that Raf-1 can be activated by chemical-induced oligomerization. However, while Farrar et al. [45•] found that the activation of Raf-1 by oligomerization is Ras-independent, Luo et al. [46•] found that an interaction with Ras is required.
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    • In this paper, the interaction between Ras and Raf-1 in NIH3T3 cells is found to localize Raf-1 to the plasma membrane for activation mediated by oncogenic Src. This Src-mediated activation involves the phosphorylation of tyrosine residues 340 and 341, This paper also shows that Raf-1 is activated by mechanisms other than tyrosine phosphorylation
    • Marais R, Light Y, Paterson HF, Marshall CJ: Ras recruits Raf-1 to the plasma membrane for activation by tyrosine phosphorylation. EMBO J 1995, 14:3136-3145. In this paper, the interaction between Ras and Raf-1 in NIH3T3 cells is found to localize Raf-1 to the plasma membrane for activation mediated by oncogenic Src. This Src-mediated activation involves the phosphorylation of tyrosine residues 340 and 341, This paper also shows that Raf-1 is activated by mechanisms other than tyrosine phosphorylation.
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    • Binding of human immunodeficiency virus type 1 to CD4 induces association of Lck and Raf-1 and activates Raf-1 by a Ras-independent pathway
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    • The cytokine-activated tyrosine kinase JAK2 activates Raf-1 in a p21 ras-dependent manner
    • This paper couples the cytokine receptor family to the Raf-1/MAPK cascade. Using the baculovirus expression system, this study shows that JAK-2 can associate with and activate Raf-1 in a manner that is Ras-dependent and that may involve the tyrosine phosphorylation of Raf-1
    • Xia K, Mukhopadhyay NK, Inhorn RC, Barber DL, Rose PE, Lee RS, Narsimhan RP, Dandrea AD, Griffin JD, Roberts TM: The cytokine-activated tyrosine kinase JAK2 activates Raf-1 in a p21 ras-dependent manner. Proc Natl Acad Sci USA 1996, 93:11681-11686. This paper couples the cytokine receptor family to the Raf-1/MAPK cascade. Using the baculovirus expression system, this study shows that JAK-2 can associate with and activate Raf-1 in a manner that is Ras-dependent and that may involve the tyrosine phosphorylation of Raf-1.
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    • Xia, K.1    Mukhopadhyay, N.K.2    Inhorn, R.C.3    Barber, D.L.4    Rose, P.E.5    Lee, R.S.6    Narsimhan, R.P.7    Dandrea, A.D.8    Griffin, J.D.9    Roberts, T.M.10
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    • 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, Kuroda S, Shimizu K, Fukui K, Ohtsuka T, Takai Y: 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 1995, 270:11723-11726.
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    • αi/o subunits
    • This paper is one of the first to address the mechanisms by which Raf-1 activity is downmodulated. A GTP-regulated protein tyrosine phosphatase that inactivates membrane-associated Raf-1 is characterized
    • αi/o subunits. J Biol Chem 1996, 271:3119-3123. This paper is one of the first to address the mechanisms by which Raf-1 activity is downmodulated. A GTP-regulated protein tyrosine phosphatase that inactivates membrane-associated Raf-1 is characterized.
    • (1996) J Biol Chem , vol.271 , pp. 3119-3123
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.