Normal and oncogenic p21ras proteins bind to the amino-terminal regulatory domain of c-Raf-1
XF Zhang, J Settleman, J Kyriakis, E Takeuchi-Suzuki… - Nature, 1993 - nature.com
XF Zhang, J Settleman, J Kyriakis, E Takeuchi-Suzuki, SJ Elledge, MS Marshall, JT Bruder…
Nature, 1993•nature.comIn 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.
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.
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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