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MAMMALIAN RAS INTERACTS DIRECTLY WITH THE SERINE THREONINE KINASE RAF
Author(s): VOJTEK AB, HOLLENBERG SM, COOPER JA
Source: CELL    Volume: 74    Issue: 1    Pages: 205-214    Published: JUL 16 1993  
Times Cited: 1,520     References: 73     
Abstract: We have identified proteins that interact with H-Ras using a two hybrid system screen of a mouse cDNA library. Approximately 50% of the clones identified encoded portions of the c-Raf and A-Raf serine/threonine kinases. Overlaps among these clones define a conserved 81 residue region of the N-terminus of Raf as the Ras interaction region. We show that Raf interacts with wild-type and activated Ras, but not with an effector domain mutant of Ras or with a dominant-interfering Ras mutant. Using purified bacterially expressed fusion proteins, we show, furthermore, that Ras and the N-terminal region of Raf associate directly in vitro and that this interaction is dependent on GTP bound to Ras.
Document Type: Article
Language: English
Reprint Address: VOJTEK, AB (reprint author), FRED HUTCHINSON CANC RES CTR, 1124 COLUMBIA ST, SEATTLE, WA 98104 USA
Publisher: CELL PRESS, 1050 MASSACHUSETTES AVE, CIRCULATION DEPT, CAMBRIDGE, MA 02138
Subject Category: Biochemistry & Molecular Biology; Cell Biology
IDS Number: LN625
ISSN: 0092-8674
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