Nature. 1993 Jul 22;364(6435):308-13.

Normal and oncogenic p21ras proteins bind to the amino-terminal regulatory domain of c-Raf-1.

Zhang XF, Settleman J, Kyriakis JM, Takeuchi-Suzuki E, Elledge SJ, Marshall MS, Bruder JT, Rapp UR, Avruch J.

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Diabetes Unit, Harvard Medical School, Charlestown, Massachusetts.

Abstract

In higher eukaryotes, the Ras and Raf-1 proto-oncoproteins transduce growth and differentiation signals initiated by tyrosine kinases. The Ras polypeptide and the amino-terminal regulatory domain of Raf-1 (residues 1-257) are shown to interact, directly in vitro and in a yeast expression system. Raf-1 (1-257) binds GTP-Ras in preference to GDP-Ras, and inhibits Ras-GAP activity. Mutations in and around the Ras effector domain impair Ras binding to Raf-1 (1-257) and Ras transforming activity in parallel.

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Normal and oncogenic p21ras proteins bind to the amino-terminal regulatory domai...
Normal and oncogenic p21ras proteins bind to the amino-terminal regulatory domain of c-Raf-1.
Nature. 1993 Jul 22 ;364(6435):308-13.

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