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Science 18 December 1992:
Vol. 258. no. 5090, pp. 1941 - 1944
DOI: 10.1126/science.1470918
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Articles

Science, Vol 258, Issue 5090, 1941-1944
Copyright © 1992 by American Association for the Advancement of Science

articles

Targeted degradation of c-Fos, but not v-Fos, by a phosphorylation-dependent signal on c-Jun

AG Papavassiliou, M Treier, C Chavrier, and D Bohmann

European Molecular Biology Laboratory, Differentiation Program, Heidelberg, Germany.

The proto-oncogene products c-Fos and c-Jun heterodimerize through their leucine zippers to form the AP-1 transcription factor. The transcriptional activity of the heterodimer is regulated by signal-dependent phosphorylation and dephosphorylation events. The stability of c-Fos was found to also be controlled by intracellular signal transduction. In transient expression and in vitro degradation experiments, the stability of c-Fos was decreased when the protein was dimerized with phosphorylated c-Jun. c-Jun protein isolated from phorbol ester-induced cells did not target c-Fos for degradation, which suggests that c-Fos is transiently stabilized after stimulation of cell growth. v-Fos protein, the retroviral counterpart of c-Fos, was not susceptible to degradation targeted by c-Jun.


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Science. ISSN 0036-8075 (print), 1095-9203 (online)