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1
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0028175091
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Raf meets Ras: Completing the framework of a signal transduction pathway
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Avruch J, Zhang X, Kyriakis JM: Raf meets Ras: completing the framework of a signal transduction pathway. Trends Biochem Sci 1994, 19:279-283.
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Trends Biochem Sci
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Avruch, J.1
Zhang, X.2
Kyriakis, J.M.3
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2
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0028104204
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The ins and outs of Raf kinases
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Daum G, Eisenmann-Tappe I, Fries H, Troppmair J, Rapp UR: The ins and outs of Raf kinases. Trends Biochem Sci 1994, 19:474-479.
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Trends Biochem Sci
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Daum, G.1
Eisenmann-Tappe, I.2
Fries, H.3
Troppmair, J.4
Rapp, U.R.5
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3
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0025277489
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Mutational activation of c-raf-1 and definition of the minimal transforming sequence
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Heidecker G, Huleihel M, Cleveland JL, Kolch W, Beck TW, Lloyd P, Pawson T, Rapp UR: Mutational activation of c-raf-1 and definition of the minimal transforming sequence. Mol Cell Biol 1990, 10:2503-2512.
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Mol Cell Biol
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Heidecker, G.1
Huleihel, M.2
Cleveland, J.L.3
Kolch, W.4
Beck, T.W.5
Lloyd, P.6
Pawson, T.7
Rapp, U.R.8
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4
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0024545162
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Definition of the human raf amino-terminal regulatory region by deletion mutagenesis
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Stanton VP Jr, Nichols DW, Laudano AP, Cooper GM: Definition of the human raf amino-terminal regulatory region by deletion mutagenesis. Mol Cell Biol 1989, 9:639-647.
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Mol Cell Biol
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Stanton V.P., Jr.1
Nichols, D.W.2
Laudano, A.P.3
Cooper, G.M.4
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5
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0028241533
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Activation of Raf as a result of recruitment to the plasma membrane
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Stokoe D, Macdonald SG, Cadwallader K, Symons M, Hancock JF: Activation of Raf as a result of recruitment to the plasma membrane. Science 1994, 26:1463-1467.
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(1994)
Science
, vol.26
, pp. 1463-1467
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Stokoe, D.1
Macdonald, S.G.2
Cadwallader, K.3
Symons, M.4
Hancock, J.F.5
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6
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0028272507
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Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane
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Leevers SJ, Paterson HF, Marshall CJ: Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane. Nature 1994, 9:411-414.
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(1994)
Nature
, vol.9
, pp. 411-414
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Leevers, S.J.1
Paterson, H.F.2
Marshall, C.J.3
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7
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0027250250
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Mammalian Ras interacts directly with the serine/threonine kinase Raf
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Vojitek AB, Hollenberg SM, Cooper JA: Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell 1993, 74:205-214.
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(1993)
Cell
, vol.74
, pp. 205-214
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Vojitek, A.B.1
Hollenberg, S.M.2
Cooper, J.A.3
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8
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0029107760
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The 2.2 Ȧ crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1a and a GTP analogue
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This paper reports the crystal structure of the Raf-1 RBD complexed to the effector domain of the Ras subfamily member Rap1A
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Nassar N, Horn G, Herrmann C, Scherer A, McCormick F, Wittinghofer A: The 2.2 Ȧ crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue. Nature 1995, 375:554-560. This paper reports the crystal structure of the Raf-1 RBD complexed to the effector domain of the Ras subfamily member Rap1A.
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(1995)
Nature
, vol.375
, pp. 554-560
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Nassar, N.1
Horn, G.2
Herrmann, C.3
Scherer, A.4
McCormick, F.5
Wittinghofer, A.6
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9
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0029864175
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Equilibrium and kinetic measurements reveal rapidly reversible binding of Ras to Raf
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Gorman C, Skinner RH, Skelly JV, Neidle S, Lowe PN: Equilibrium and kinetic measurements reveal rapidly reversible binding of Ras to Raf. J Biol Chem 1996, 271:6713-6719.
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(1996)
J Biol Chem
, vol.271
, pp. 6713-6719
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Gorman, C.1
Skinner, R.H.2
Skelly, J.V.3
Neidle, S.4
Lowe, P.N.5
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10
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0028795913
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Quantitative analysis of the complex between p21ras and the Ras-binding domain of the human Raf-1 protein kinase
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Herrmann C, Martin GA, Wittinghofer A: Quantitative analysis of the complex between p21ras and the Ras-binding domain of the human Raf-1 protein kinase. J Biol Chem 1995, 270:2901-2905.
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(1995)
J Biol Chem
, vol.270
, pp. 2901-2905
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Herrmann, C.1
Martin, G.A.2
Wittinghofer, A.3
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11
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0029913467
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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
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This paper examines the affinity and specificity of binding between different members of the Ras subfamily and various Ras effectors
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Herrmann C, Horn G, Spaargaren M, Wittinghofer A: 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 1996, 271:6794-6800. This paper examines the affinity and specificity of binding between different members of the Ras subfamily and various Ras effectors.
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(1996)
J Biol Chem
, vol.271
, pp. 6794-6800
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Herrmann, C.1
Horn, G.2
Spaargaren, M.3
Wittinghofer, A.4
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12
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0029879058
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Quantitative structure-activity analysis correlating Ras/Raf interaction in vitro to Raf activation in vivo
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A quantitative analysis, using mutants of Raf-1 to correlate the affinity of the Ras-Raf-1 interaction in vitro with Raf-1 activity in vivo. This study identifies key residues of Raf-1 that determine the binding affinity of the RBD to the Ras effector domain
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Block C, Janknecht R, Herrmann C, Nassar N, Wittinghofer A: Quantitative structure-activity analysis correlating Ras/Raf interaction in vitro to Raf activation in vivo. Nat Struct Biol 1996,3:244-251. A quantitative analysis, using mutants of Raf-1 to correlate the affinity of the Ras-Raf-1 interaction in vitro with Raf-1 activity in vivo. This study identifies key residues of Raf-1 that determine the binding affinity of the RBD to the Ras effector domain.
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Nat Struct Biol 1996
, vol.3
, pp. 244-251
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Block, C.1
Janknecht, R.2
Herrmann, C.3
Nassar, N.4
Wittinghofer, A.5
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13
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0028956033
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Two distinct Raf domains mediate interaction with Ras
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Brtva TR, Drugan JK, Ghosh S, Terrell RS, Campbell-Burk S, Bell RM, Der CJ: Two distinct Raf domains mediate interaction with Ras. J Biol Chem 1995, 270:9809-9812.
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(1995)
J Biol Chem
, vol.270
, pp. 9809-9812
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Brtva, T.R.1
Drugan, J.K.2
Ghosh, S.3
Terrell, R.S.4
Campbell-Burk, S.5
Bell, R.M.6
Der, C.J.7
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14
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0030053105
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Ras interaction with two distinct binding domains in Raf-1 may be required for Ras transformation
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See annotation [15••]
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Drugan JK, Khosravi-Far R, White MA, Der CJ, Sung Y, Hwang Y, Campbell S: Ras interaction with two distinct binding domains in Raf-1 may be required for Ras transformation. J Biol Chem 1996, 271:233-237. See annotation [15••].
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(1996)
J Biol Chem
, vol.271
, pp. 233-237
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Drugan, J.K.1
Khosravi-Far, R.2
White, M.A.3
Der, C.J.4
Sung, Y.5
Hwang, Y.6
Campbell, S.7
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15
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0029587739
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Cysteine-rich region of Raf-1 interacts with activator domain of post-translationally modified Ha-Ras
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These two papers [14••,15••] demonstrate that Raf-1 contains two distinct Ras-binding domains, each of which recognizes distinct Ras determinants. One domain is the well characterized RBD and the second encompasses the cysteine-rich domain of Raf-1
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Hu C, Kariya K, Tamada M, Akasaka K, Shirouzu M, Yokoyama S, Kataoka T: Cysteine-rich region of Raf-1 interacts with activator domain of post-translationally modified Ha-Ras. J Biol Chem 1995, 270:30274-30277. These two papers [14••,15••] demonstrate that Raf-1 contains two distinct Ras-binding domains, each of which recognizes distinct Ras determinants. One domain is the well characterized RBD and the second encompasses the cysteine-rich domain of Raf-1.
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(1995)
J Biol Chem
, vol.270
, pp. 30274-30277
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Hu, C.1
Kariya, K.2
Tamada, M.3
Akasaka, K.4
Shirouzu, M.5
Yokoyama, S.6
Kataoka, T.7
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16
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0029757119
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The solution structure of the Raf-1 cysteine-rich domain: A novel Ras and phospholipid binding site
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This paper presents the NMR-derived solution structure of the Raf-1 CRD. Comparisons are made between the Raf-1 CRD and the related domains of two PKC isoforms
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Mott HR, Carpenter JW, Zhong S, Ghosh S, Bell RM, Campbell SL: The solution structure of the Raf-1 cysteine-rich domain: a novel Ras and phospholipid binding site. Proc Natl Acad Sci USA 1996, 93:8312-8317. This paper presents the NMR-derived solution structure of the Raf-1 CRD. Comparisons are made between the Raf-1 CRD and the related domains of two PKC isoforms.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 8312-8317
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Mott, H.R.1
Carpenter, J.W.2
Zhong, S.3
Ghosh, S.4
Bell, R.M.5
Campbell, S.L.6
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17
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0029071689
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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
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This study demonstrates that Raf-1 serine phosphorylation is required for the interaction with the 14-3-3 protein. Data are also presented that show that Raf-1 proteins that are unable to stably interact with 14-3-3 are activated, implicating a role for 14-3-3 in stabilizing the inactive conformation of Raf-1
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Michaud NR, Fabian JR, Mathes KD, Morrison DK: 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 1995, 15:3390-3397. This study demonstrates that Raf-1 serine phosphorylation is required for the interaction with the 14-3-3 protein. Data are also presented that show that Raf-1 proteins that are unable to stably interact with 14-3-3 are activated, implicating a role for 14-3-3 in stabilizing the inactive conformation of Raf-1.
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(1995)
Mol Cell Biol
, vol.15
, pp. 3390-3397
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Michaud, N.R.1
Fabian, J.R.2
Mathes, K.D.3
Morrison, D.K.4
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18
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0028083893
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The cysteine-rich region of Raf-1 kinase contains zinc, translocates to liposomes and is adjacent to a segment that bind GTP-Ras
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Ghosh S, Xiw WQ, Quest AFG, Mabrouk GM, Sturm JC, Bell RM: The cysteine-rich region of Raf-1 kinase contains zinc, translocates to liposomes and is adjacent to a segment that bind GTP-Ras. J Biol Chem 1994, 269:10000-10007.
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(1994)
J Biol Chem
, vol.269
, pp. 10000-10007
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-
Ghosh, S.1
Xiw, W.Q.2
Quest, A.F.G.3
Mabrouk, G.M.4
Sturm, J.C.5
Bell, R.M.6
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19
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0029951162
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Ceramide-binding and activation defines protein kinase c-Raf as a ceramide-activated protein kinase
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This paper reports that ceramide specifically binds to and activates Raf-1. These findings suggest that ceramide may be an authentic lipid activator of Raf-1 in signaling pathways in which ceramide production is induced
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Huwiler A, Brunner J, Hummel R, Vervoordeldonk M, Stabel S, Van Den Bosch H, Pfeilschifter J: Ceramide-binding and activation defines protein kinase c-Raf as a ceramide-activated protein kinase. Proc Natl Acad Sci USA 1996, 93:6959-6963. This paper reports that ceramide specifically binds to and activates Raf-1. These findings suggest that ceramide may be an authentic lipid activator of Raf-1 in signaling pathways in which ceramide production is induced.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 6959-6963
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Huwiler, A.1
Brunner, J.2
Hummel, R.3
Vervoordeldonk, M.4
Stabel, S.5
Van Den Bosch, H.6
Pfeilschifter, J.7
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20
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0028973293
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Ras CAAX peptidomimetic FTI-277 selectively blocks oncogenic Ras signaling by inducing cytoplasmic accumulation of inactive Ras-Raf complexes
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Using inhibitors of farnesyltransferase, this study shows that Raf-1 bound to unfarnesylated Ras in the cytosol is inactive. This paper, together with [21•], emphasizes the importance of farnesylation to the ability of Ras to activate Raf proteins
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Lerner EC, Qian Y, Blaskovich MA, Fossum RD, Vogt A, Sun J, Cox AD, Der CJ, Hamilton AD, Sebti SM: Ras CAAX peptidomimetic FTI-277 selectively blocks oncogenic Ras signaling by inducing cytoplasmic accumulation of inactive Ras-Raf complexes. J Biol Chem 1995, 270:26802-26806, Using inhibitors of farnesyltransferase, this study shows that Raf-1 bound to unfarnesylated Ras in the cytosol is inactive. This paper, together with [21•], emphasizes the importance of farnesylation to the ability of Ras to activate Raf proteins.
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(1995)
J Biol Chem
, vol.270
, pp. 26802-26806
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Lerner, E.C.1
Qian, Y.2
Blaskovich, M.A.3
Fossum, R.D.4
Vogt, A.5
Sun, J.6
Cox, A.D.7
Der, C.J.8
Hamilton, A.D.9
Sebti, S.M.10
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21
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0029919472
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Post-translational modification of H-Ras is reauired for activation of, but not for association with, B-Raf
-
This paper finds that, although unfarnesylated Ras can bind B-Raf, only farnesylated Ras can activate B-Raf in an in vitro activation system. See also [120•]
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Okada T, Masuda T, Shinkai M, Kariya K, Kataoka T: Post-translational modification of H-Ras is reauired for activation of, but not for association with, B-Raf. J Biol Chem 1996, 271:4671-4678. This paper finds that, although unfarnesylated Ras can bind B-Raf, only farnesylated Ras can activate B-Raf in an in vitro activation system. See also [120•].
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(1996)
J Biol Chem
, vol.271
, pp. 4671-4678
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Okada, T.1
Masuda, T.2
Shinkai, M.3
Kariya, K.4
Kataoka, T.5
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22
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0029866641
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Peptides containing a consensus Ras binding sequence from Raf-1 and the GTPase activating protein NF1 inhibit Ras function
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Clark GJ, Drugan JK, Terrell RS, Bradham C, Der CJ, Bell RM, Campbell S: Peptides containing a consensus Ras binding sequence from Raf-1 and the GTPase activating protein NF1 inhibit Ras function. Proc Natl Acad Sci USA 1996, 93:1577-1581.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 1577-1581
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Clark, G.J.1
Drugan, J.K.2
Terrell, R.S.3
Bradham, C.4
Der, C.J.5
Bell, R.M.6
Campbell, S.7
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23
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0027161398
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Complex formation between Ras and Raf and other protein kinases
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Van Aelst L, Barr M, Marcus S, Polverino A, Wigler M: Complex formation between Ras and Raf and other protein kinases. Proc Natl Acad Sci USA 1993, 90:6213-6217.
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(1993)
Proc Natl Acad Sci USA
, vol.90
, pp. 6213-6217
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Van Aelst, L.1
Barr, M.2
Marcus, S.3
Polverino, A.4
Wigler, M.5
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24
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0029164688
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A proline-rich sequence unique to MEK1 and MEK2 is required for Raf binding and regulates MEK function
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This paper reports that MEK1 and MEK2 contain a unique proline-rich sequence that is required for Raf-1 binding. This sequence may be a recognition motif involved in directing specific MEK-protein interactions
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Catling AD, Schaefffer H, Reuter CWM, Reddy GR, Weber MJ: A proline-rich sequence unique to MEK1 and MEK2 is required for Raf binding and regulates MEK function. Mol Cell Biol 1995, 15:5214-5225. This paper reports that MEK1 and MEK2 contain a unique proline-rich sequence that is required for Raf-1 binding. This sequence may be a recognition motif involved in directing specific MEK-protein interactions.
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(1995)
Mol Cell Biol
, vol.15
, pp. 5214-5225
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Catling, A.D.1
Schaefffer, H.2
Reuter, C.W.M.3
Reddy, G.R.4
Weber, M.J.5
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25
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0028032296
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14-3-3: Modulators of signaling proteins?
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Morrison D: 14-3-3: modulators of signaling proteins? Science 1994, 266:56-57.
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(1994)
Science
, vol.266
, pp. 56-57
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Morrison, D.1
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26
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0028051904
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Stimulatory effects of yeast and mammalian 14-3-3 proteins on the Raf protein kinase
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Irie K, Gotoh Y, Yashar BM, Errede B, Nishida E, Matsumoto K: Stimulatory effects of yeast and mammalian 14-3-3 proteins on the Raf protein kinase. Science 1994, 265:1716-1719.
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(1994)
Science
, vol.265
, pp. 1716-1719
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Irie, K.1
Gotoh, Y.2
Yashar, B.M.3
Errede, B.4
Nishida, E.5
Matsumoto, K.6
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27
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0027944852
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Activation of Raf-1 by 14-3-3 proteins
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Fantl WJ, Muslin AJ, Kikuchi A, Martin JA, MacNicol AM, Gross RW, Williams LT: Activation of Raf-1 by 14-3-3 proteins. Nature 1994, 371:612-613.
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(1994)
Nature
, vol.371
, pp. 612-613
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-
Fantl, W.J.1
Muslin, A.J.2
Kikuchi, A.3
Martin, J.A.4
MacNicol, A.M.5
Gross, R.W.6
Williams, L.T.7
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28
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0028073606
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Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation
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Freed E, Symons M, Macdonald SG, McCormick F, Ruggieri R: Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation. Science 1994, 265:1713-1716.
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(1994)
Science
, vol.265
, pp. 1713-1716
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Freed, E.1
Symons, M.2
Macdonald, S.G.3
McCormick, F.4
Ruggieri, R.5
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29
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0030248429
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14-3-3 and its possible role in co-ordinating multiple signalling pathways
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A thorough review examining the function of 14-3-3 in multiple signaling pathways
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Aitken A: 14-3-3 and its possible role in co-ordinating multiple signalling pathways. Trends Cell Biol 1996, 6:341-347. A thorough review examining the function of 14-3-3 in multiple signaling pathways.
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(1996)
Trends Cell Biol
, vol.6
, pp. 341-347
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Aitken, A.1
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30
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0029871708
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Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
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This paper demonstrates that 14-3-3 is a specific phosphoserine-binding protein, and defines a phosphorylation-dependent 14-3-3-binding motif (RSxS*xP [single-letter code for amino acids; x represents any amino acid and S* represents phosphorylated serine]). These findings reveal that serine-phosphorylated residues, like tyrosine-phosphorylated residues, can act as recognition sites for protein interactions
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Muslin AJ, Tanner JW, Allen PM, Shaw AS: Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 1996, 84:889-897. This paper demonstrates that 14-3-3 is a specific phosphoserine-binding protein, and defines a phosphorylation-dependent 14-3-3-binding motif (RSxS*xP [single-letter code for amino acids; x represents any amino acid and S* represents phosphorylated serine]). These findings reveal that serine-phosphorylated residues, like tyrosine-phosphorylated residues, can act as recognition sites for protein interactions.
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(1996)
Cell
, vol.84
, pp. 889-897
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Muslin, A.J.1
Tanner, J.W.2
Allen, P.M.3
Shaw, A.S.4
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31
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0027168907
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Identification of the major phosphorylation sites of the Raf-1 kinase
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Morrison DK, Heidecker G, Rapp UR, Copeland TD: Identification of the major phosphorylation sites of the Raf-1 kinase. J Biol Chem 1993, 268:17309-17316.
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(1993)
J Biol Chem
, vol.268
, pp. 17309-17316
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Morrison, D.K.1
Heidecker, G.2
Rapp, U.R.3
Copeland, T.D.4
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32
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0030064432
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Activated Ras displaces 14-3-3 protein from the amino terminus of c-Raf-1
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Rommel C, Radziwill G, Lovric J, Noeldeke J, Heinicke T, Jones D, Aitken A, Moelling K: Activated Ras displaces 14-3-3 protein from the amino terminus of c-Raf-1. Oncogene 1996, 12:609-619.
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(1996)
Oncogene
, vol.12
, pp. 609-619
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-
Rommel, C.1
Radziwill, G.2
Lovric, J.3
Noeldeke, J.4
Heinicke, T.5
Jones, D.6
Aitken, A.7
Moelling, K.8
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33
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0029014973
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Reversal of Raf-1 activation by purified and membrane-associated protein phosphatases
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This paper reports that activated Raf-1 can be inactivated by both serine/threonine- and tyrosine-specific phosphatases, and that the dephosphorylation and inactivation of Raf-1 can be blocked by the binding of 14-3-3 and hsp90
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Dent P, Jelinek T, Morrison DK, Weber MJ, Sturgill TW: Reversal of Raf-1 activation by purified and membrane-associated protein phosphatases. Science 1995, 268:1902-1906. This paper reports that activated Raf-1 can be inactivated by both serine/threonine- and tyrosine-specific phosphatases, and that the dephosphorylation and inactivation of Raf-1 can be blocked by the binding of 14-3-3 and hsp90.
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(1995)
Science
, vol.268
, pp. 1902-1906
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Dent, P.1
Jelinek, T.2
Morrison, D.K.3
Weber, M.J.4
Sturgill, T.W.5
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34
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0028979375
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Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways
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See annotation [35•]
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Xiao B, Smerdon SJ, Jones DH, Dodson GG, Soneji Y, Aitken A, Gamblin SJ: Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways. Nature 1995, 376:188-191. See annotation [35•].
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(1995)
Nature
, vol.376
, pp. 188-191
-
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Xiao, B.1
Smerdon, S.J.2
Jones, D.H.3
Dodson, G.G.4
Soneji, Y.5
Aitken, A.6
Gamblin, S.J.7
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35
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0029046812
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Crystal structure of the zeta isoform of the 14-3-3 protein
-
These two papers [34•,35•] present the crystal structures of two different isoforms of 14-3-3, namely C and T. Both isoforms were able to form dimers, and the residues in the dimer interface were found to be invariant among all 14-3-3 isoforms, indicating the potential for the formation of heterodimers and larger protein complexes
-
Liu D, Bienkowska J, Petoa C, Collier RJ, Fu H, Liddington R: Crystal structure of the zeta isoform of the 14-3-3 protein. Nature 1995, 376:191-194. These two papers [34•,35•] present the crystal structures of two different isoforms of 14-3-3, namely C and T. Both isoforms were able to form dimers, and the residues in the dimer interface were found to be invariant among all 14-3-3 isoforms, indicating the potential for the formation of heterodimers and larger protein complexes.
-
(1995)
Nature
, vol.376
, pp. 191-194
-
-
Liu, D.1
Bienkowska, J.2
Petoa, C.3
Collier, R.J.4
Fu, H.5
Liddington, R.6
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36
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0029166558
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BCR and RAF form a complex in vivo via 14-3-3 proteins
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Braselmann S, McCormick F: BCR and RAF form a complex in vivo via 14-3-3 proteins. EMBO J 1995, 14:4839-4848.
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(1995)
EMBO J
, vol.14
, pp. 4839-4848
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Braselmann, S.1
McCormick, F.2
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38
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0029829237
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14-3-3 proteins associate with A20 in an isoform-specific manner and function both as chaperone and adaptor molecules
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Vincenz C, Dixit V: 14-3-3 proteins associate with A20 in an isoform-specific manner and function both as chaperone and adaptor molecules. J Biol Chem 1996, 271:20029-20034.
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(1996)
J Biol Chem
, vol.271
, pp. 20029-20034
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Vincenz, C.1
Dixit, V.2
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39
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0029163251
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14-3-3 proteins: Biological function and domain structure
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Aitken A, Jones D, Soneji Y, Howell S: 14-3-3 proteins: biological function and domain structure. Biochem Soc Trans 1995, 23:605-611.
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(1995)
Biochem Soc Trans
, vol.23
, pp. 605-611
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Aitken, A.1
Jones, D.2
Soneji, Y.3
Howell, S.4
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40
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0028227245
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The native structure of the activated Raf protein kinase is a membrane-bound multi-subunit complex
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Wartmann M, Davis RJ: The native structure of the activated Raf protein kinase is a membrane-bound multi-subunit complex. J Biol Chem 1994, 269:6695-6701.
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(1994)
J Biol Chem
, vol.269
, pp. 6695-6701
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Wartmann, M.1
Davis, R.J.2
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41
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0029665779
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Mammalian p50 Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4
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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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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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(1996)
Genes Dev
, vol.10
, pp. 1491-1502
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Stepanova, L.1
Leng, X.2
Parker, S.B.3
Harper, J.W.4
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42
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0028786332
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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
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See annotation [43•]
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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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(1995)
J Biol Chem
, vol.270
, pp. 24585-24588
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Schulte, T.W.1
Blagosklonny, M.V.2
Ingui, C.3
Neckers, L.4
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43
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0029813620
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Destabilization of Raf-1 by geldanamycin leads to disruption of the Raf-1-MEK-mitogen-activated protein kinase signalling pathway
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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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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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(1996)
Mol Cell Biol
, vol.16
, pp. 5839-5845
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Schulte, T.W.1
Blagosklonny, M.V.2
Romanova, L.3
Mushinski, J.F.4
Monia, B.P.5
Johnston, J.F.6
Nguyen, P.7
Trepel, J.8
Neckers, L.M.9
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44
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0029850713
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KSR modulates signal propagation within the MAPK cascade
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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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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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(1996)
Genes Dev
, vol.10
, pp. 2684-2695
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Therrien, M.1
Michaud, N.R.2
Rubin, G.M.3
Morrison, D.K.4
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45
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0029807304
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Activation of the Raf-1 kinase cascade by coumermycin-induced dimerization
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See annotation [46•]
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Farrar MA, Alberola-lla J, Perlmutter RM: Activation of the Raf-1 kinase cascade by coumermycin-induced dimerization. Nature 1996, 383:178-181. See annotation [46•].
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(1996)
Nature
, vol.383
, pp. 178-181
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Farrar, M.A.1
Alberola-lla, J.2
Perlmutter, R.M.3
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46
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0029811985
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Oligomerization activates c-Raf-1 through a Ras-dependent mechanism
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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
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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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(1996)
Nature
, vol.383
, pp. 181-185
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Luo, Z.1
Tzivion, G.2
Belshaw, P.J.3
Vawas, D.4
Marshall, M.5
Avruch, J.6
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47
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0027935756
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Interaction of Ras and Raf in intact mammalian cells upon extracellular stimulation
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Hallberg B, Rayter SI, Downward J: Interaction of Ras and Raf in intact mammalian cells upon extracellular stimulation. J Biol Chem 1994, 269:3913-3916.
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(1994)
J Biol Chem
, vol.269
, pp. 3913-3916
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Hallberg, B.1
Rayter, S.I.2
Downward, J.3
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48
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0027364980
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Critical tyrosine residues regulate the enzymatic and biological activity of Raf-1 kinase
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Fabian JR, Daar IO, Morrison DK: Critical tyrosine residues regulate the enzymatic and biological activity of Raf-1 kinase. Mol Cell Biol 1993, 13:7170-7179.
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(1993)
Mol Cell Biol
, vol.13
, pp. 7170-7179
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Fabian, J.R.1
Daar, I.O.2
Morrison, D.K.3
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49
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0029006126
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Ras recruits Raf-1 to the plasma membrane for activation by tyrosine phosphorylation
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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
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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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(1995)
EMBO J
, vol.14
, pp. 3136-3145
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Marais, R.1
Light, Y.2
Paterson, H.F.3
Marshall, C.J.4
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50
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0029802684
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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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Popik W, Pitha PM: 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. Mol Cell Biol 1996, 16:6532-6541.
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(1996)
Mol Cell Biol
, vol.16
, pp. 6532-6541
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Popik, W.1
Pitha, P.M.2
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51
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0029920272
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A role for Shc, Grb2, and Raf-1 in FcγRI signal relay
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Park RK, Liu Y, Durden DL: A role for Shc, Grb2, and Raf-1 in FcγRI signal relay. J Biol Chem 1996, 271:13342-13348.
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(1996)
J Biol Chem
, vol.271
, pp. 13342-13348
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Park, R.K.1
Liu, Y.2
Durden, D.L.3
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52
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0029737462
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Activation of Raf by ionizing radiation
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Kasid U, Suy S, Dent P, Ray S, Whiteside TL, Sturgill TW: Activation of Raf by ionizing radiation. Nature 1996, 382:813-816.
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(1996)
Nature
, vol.382
, pp. 813-816
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Kasid, U.1
Suy, S.2
Dent, P.3
Ray, S.4
Whiteside, T.L.5
Sturgill, T.W.6
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53
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0029954969
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The cytokine-activated tyrosine kinase JAK2 activates Raf-1 in a p21 ras-dependent manner
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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, 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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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 11681-11686
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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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54
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0027326410
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Protein kinase Ca activates Raf-1 by direct phosphorylation
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Kolch W, Heidecker G, Kochs G, Hummel R, Vahidi H, Mischak H, Finkenzeller G, Marme D, Rapp UR: Protein kinase Ca activates Raf-1 by direct phosphorylation. Nature 1993, 364:249-252.
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(1993)
Nature
, vol.364
, pp. 249-252
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Kolch, W.1
Heidecker, G.2
Kochs, G.3
Hummel, R.4
Vahidi, H.5
Mischak, H.6
Finkenzeller, G.7
Marme, D.8
Rapp, U.R.9
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55
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0028057469
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Protein kinase C-mediated serine phosphorylation directly activates Raf-1 in murine hematopoietic cells
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Carroll MP, May WS: Protein kinase C-mediated serine phosphorylation directly activates Raf-1 in murine hematopoietic cells. J Biol Chem 1994, 269:1249-1256.
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(1994)
J Biol Chem
, vol.269
, pp. 1249-1256
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Carroll, M.P.1
May, W.S.2
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56
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0029789967
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Protein kinase C δ activates the MEK-ERK pathway in a manner independent of Ras and dependent on Raf
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Ueda Y, Hirai S, Osada S, Suzuki A, Mizuno K, Ohno S: Protein kinase C δ activates the MEK-ERK pathway in a manner independent of Ras and dependent on Raf. J Biol Chem 1996, 271:23512-23519.
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(1996)
J Biol Chem
, vol.271
, pp. 23512-23519
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Ueda, Y.1
Hirai, S.2
Osada, S.3
Suzuki, A.4
Mizuno, K.5
Ohno, S.6
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57
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0028838235
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Phosphorylation of Raf by ceramide-activated protein kinase
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Yao B, Zhang Y, Delikat S, Mathias S, Basu S, Kolesnick R: Phosphorylation of Raf by ceramide-activated protein kinase. Nature 1995, 378:307-310.
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(1995)
Nature
, vol.378
, pp. 307-310
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Yao, B.1
Zhang, Y.2
Delikat, S.3
Mathias, S.4
Basu, S.5
Kolesnick, R.6
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58
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0028124505
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Mechanism of inhibition of Raf-1 by protein kinase A
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Hafner S, Adler HS, Mischak H, Janosch P, Heidecker G, Wolfman A, Pippig S, Lohse M, Ueffing M, Kolch W: Mechanism of inhibition of Raf-1 by protein kinase A. Mol Cell Biol 1994, 14:6696-6703.
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(1994)
Mol Cell Biol
, vol.14
, pp. 6696-6703
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-
Hafner, S.1
Adler, H.S.2
Mischak, H.3
Janosch, P.4
Heidecker, G.5
Wolfman, A.6
Pippig, S.7
Lohse, M.8
Ueffing, M.9
Kolch, W.10
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59
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0027385030
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Conditional transformation of cells and rapid activation of the mitogen-activated protein kinase cascade by an estradiol-dependent human Raf-1 protein kinase
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Samuels ML, Weber MJ, Bishop M, McMahon M: Conditional transformation of cells and rapid activation of the mitogen-activated protein kinase cascade by an estradiol-dependent human Raf-1 protein kinase. Mol Cell Biol 1993, 13:6241-6252.
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(1993)
Mol Cell Biol
, vol.13
, pp. 6241-6252
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-
Samuels, M.L.1
Weber, M.J.2
Bishop, M.3
McMahon, M.4
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60
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0029971008
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Identification of signalling proteins interacting with B-Raf in the yeast two-hybrid system
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Papin C, Denouel A, Calothy G, Eychene A: Identification of signalling proteins interacting with B-Raf in the yeast two-hybrid system. Oncogene 1996, 12:2213-2221.
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(1996)
Oncogene
, vol.12
, pp. 2213-2221
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Papin, C.1
Denouel, A.2
Calothy, G.3
Eychene, A.4
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61
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0029058730
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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
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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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(1995)
J Biol Chem
, vol.270
, pp. 11723-11726
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Yamamori, B.1
Kuroda, S.2
Shimizu, K.3
Fukui, K.4
Ohtsuka, T.5
Takai, Y.6
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62
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0030065773
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αi/o subunits
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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
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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.
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(1996)
J Biol Chem
, vol.271
, pp. 3119-3123
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Dent, P.1
Reardon, D.B.2
Wood, S.L.3
Lindorfer, M.A.4
Graber, S.G.5
Garrison, J.C.6
Brautigan, D.L.7
Sturgill, T.W.8
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