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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1993-07

AUTHORS

Xian-Feng Zhang, Jeffrey Settleman, John Kyriakis, Erika Takeuchi-Suzuki, Stephen J. Elledge, Mark S. Marshall, Joseph T. Bruder, Ulf R. Rapp, Joseph Avruch

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. More... »

PAGES

308-313

Journal

TITLE

Nature

ISSUE

6435

VOLUME

364

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/364308a0

DOI

http://dx.doi.org/10.1038/364308a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1021693984

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8332187


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