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Science 30 June 1995:
Vol. 268. no. 5219, pp. 1902 - 1906
DOI: 10.1126/science.7604263

Articles

Science, Vol 268, Issue 5219, 1902-1906
Copyright © 1995 by American Association for the Advancement of Science


articles

Reversal of Raf-1 activation by purified and membrane-associated protein phosphatases

P Dent, T Jelinek, DK Morrison, MJ Weber, and TW Sturgill

Howard Hughes Medical Institute, University of Virginia, Charlottesville 22908, USA.

The Raf-1 protein kinase participates in transduction of mitogenic signals, but its mechanisms of activation are incompletely understood. Treatment of human Raf-1 purified from insect Sf9 cells co-expressing c-H-Ras and Src(Y527F) (in which phenylalanine replaces tyrosine at residue 527) with either serine-threonine or tyrosine phosphatases resulted in enzymatic inactivation of Raf-1. Inactivation of purified Raf-1 was blocked by addition of either the 14-3-3 zeta protein or heat shock protein 90. Loading of plasma membranes from transformed cells with guanosine triphosphate (GTP) resulted in inactivation of endogenous or exogenous Raf-1; inactivation was blocked by inclusion of protein phosphatase inhibitors. These results suggest the existence of protein phosphatases in the cell membrane that are regulated by GTP and are responsible for Raf-1 inactivation.


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J. Biol. Chem. 271, 3119-3123
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Selective Activation of MEK1 but Not MEK2 by A-Raf from Epidermal Growth Factor-stimulated Hela Cells.
X. Wu, S. J. Noh, G. Zhou, J. E. Dixon, and K.-L. Guan (1996)
J. Biol. Chem. 271, 3265-3271
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Protein phosphatase 2A positively and negatively regulates Ras1-mediated photoreceptor development in Drosophila..
D A Wassarman, N M Solomon, H C Chang, F D Karim, M Therrien, and G M Rubin (1996)
Genes & Dev. 10, 272-278
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Identification of the Site of Interaction of the 14-3-3 Protein with Phosphorylated Tryptophan Hydroxylase.
T. Ichimura, J. Uchiyama, O. Kunihiro, M. Ito, T. Horigome, S. Omata, F. Shinkai, H. Kaji, and T. Isobe (1995)
J. Biol. Chem. 270, 28515-28518
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Hypertrophic Agonists Stimulate the Activities of the Protein Kinases c-Raf and A-Raf in Cultured Ventricular Myocytes.
M. A. Bogoyevitch, C. J. Marshall, and P. H. Sugden (1995)
J. Biol. Chem. 270, 26303-26310
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Calyculin A-induced Vimentin Phosphorylation Sequesters 14-3-3 and Displaces Other 14-3-3 Partners in Vivo.
G. Tzivion, Z.-J. Luo, and J. Avruch (2000)
J. Biol. Chem. 275, 29772-29778
   Abstract »    Full Text »    PDF »
Raf-1/MEK/MAPK Pathway Is Necessary for the G2/M Transition Induced by Nocodazole.
C. Hayne, G. Tzivion, and Z. Luo (2000)
J. Biol. Chem. 275, 31876-31882
   Abstract »    Full Text »    PDF »
14-3-3zeta Is an Effector of Tau Protein Phosphorylation.
M. Hashiguchi, K. Sobue, and H. K. Paudel (2000)
J. Biol. Chem. 275, 25247-25254
   Abstract »    Full Text »    PDF »
Kinase Suppressor of Ras Signals through Thr269 of c-Raf-1.
H. R. Xing and R. Kolesnick (2001)
J. Biol. Chem. 276, 9733-9741
   Abstract »    Full Text »    PDF »
The PTP{micro} Protein-tyrosine Phosphatase Binds and Recruits the Scaffolding Protein RACK1 to Cell-Cell Contacts.
T. Mourton, C. B. Hellberg, S. M. Burden-Gulley, J. Hinman, A. Rhee, and S. M. Brady-Kalnay (2001)
J. Biol. Chem. 276, 14896-14901
   Abstract »    Full Text »    PDF »
Serum- and Glucocorticoid-inducible Kinase SGK Phosphorylates and Negatively Regulates B-Raf.
B.-H. Zhang, E. D. Tang, T. Zhu, M. E. Greenberg, A. B. Vojtek, and K.-L. Guan (2001)
J. Biol. Chem. 276, 31620-31626
   Abstract »    Full Text »    PDF »



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