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PMID: 1903181 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Ha-Ras augments c-Jun activity and stimulates phosphorylation of its activation domain.

Nature ·Vol. 351 ·No. 6322 ·1991-05-09 ·Pages 122-7

Binétruy B, Smeal T, Karin M

Abstract

Ha-Ras augments c-Jun-mediated transactivation by potentiating the activity of the c-Jun activation domain. Ha-Ras also causes a corresponding increase in phosphorylation of specific sites in that part of the c-Jun protein. A Ha-Ras-induced protein kinase cascade resulting in hyperphosphorylation of the c-Jun activation domain could explain how these oncoproteins cooperate to transform rat embryo fibroblasts.

MeSH Terms

Animals Cell Line Chloramphenicol O-Acetyltransferase/genetics DNA-Binding Proteins/genetics,metabolism Gene Expression Regulation Phosphorylation Proto-Oncogene Proteins/genetics,metabolism Proto-Oncogene Proteins c-fos Proto-Oncogene Proteins c-jun Proto-Oncogene Proteins p21(ras)/genetics,metabolism Proto-Oncogenes/genetics Transcription Factors/genetics,metabolism Transcriptional Activation Transfection

Chemicals

DNA-Binding Proteins Proto-Oncogene Proteins Proto-Oncogene Proteins c-fos Proto-Oncogene Proteins c-jun Transcription Factors Chloramphenicol O-Acetyltransferase Proto-Oncogene Proteins p21(ras)

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Binétruy B

Department of Pharmacology, School of Medicine, University of California San Diego, La Jolla 92093.

Smeal T

Karin M

Article Info

Journal

Nature

Abbr.

Nature

ISSN

0028-0836

DOI

10.1038/351122a0

Published

1991-05-09

Pages

122-7

Language

English

Region

England

NLM ID

0410462

Subset

External Links

PubMed source DOI: 10.1038/351122a0 View journal details

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Ha-Ras augments c-Jun activity and stimulates phosphorylation of its activation domain.

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