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Science 16 September 1994:
Vol. 265. no. 5179, pp. 1716 - 1719
DOI: 10.1126/science.8085159

Articles

Science, Vol 265, Issue 5179, 1716-1719
Copyright © 1994 by American Association for the Advancement of Science


articles

Stimulatory effects of yeast and mammalian 14-3-3 proteins on the Raf protein kinase

K Irie, Y Gotoh, BM Yashar, B Errede, E Nishida, and K Matsumoto

Department of Molecular Biology, Faculty of Science, Nagoya University, Japan.

Intracellular signaling from receptor tyrosine kinases in mammalian cells results in activation of a signal cascade that includes the guanine nucleotide-binding protein Ras and the protein kinases Raf, MEK [mitogen-activated protein kinase (MAPK) or extracellular signal-regulated kinase (ERK) kinase], and MAPK. MAPK activation that is dependent on the coupling of Ras and Raf was reconstituted in yeast. Yeast genes were isolated that, when overexpressed, enhanced the function of Raf. One of them is identical to BMH1, which encodes a protein similar to members of the mammalian 14-3-3 family. Bacterially synthesized mammalian 14-3-3 protein stimulated the activity of Raf prepared from yeast cells expressing c-Raf-1. Thus, the 14-3-3 protein may participate in or be required for activation of Raf.


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PKN Associates and Phosphorylates the Head-Rod Domain of Neurofilament Protein.
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Raf-1 Kinase Possesses Distinct Binding Domains for Phosphatidylserine and Phosphatidic Acid.
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J. Biol. Chem. 271, 8472-8480
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Identification of a Binding Sequence for the 14-3-3 Protein within the Cytoplasmic Domain of the Adhesion Receptor, Platelet Glycoprotein Ibalpha.
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14-3-3: modulators of signaling proteins?.
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Proteins of the 14-3-3 Family Associate with Raf and Contribute to Its Activation.
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The Recruitment of Raf-1 to Membranes Is Mediated by Direct Interaction with Phosphatidic Acid and Is Independent of Association with Ras.
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