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

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Item Type:	Article
Title:	Targeted degradation of c-Fos, but not v-Fos, by a phosphorylation-dependent signal on c-Jun
Creators Name:	Papavassiliou, A.G., Treier, M., Chavrier, C. and Bohmann, D.
Abstract:	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.
Keywords:	Amino Acid Sequence, Codon, Genetic Transcription, HeLa Cells, Macromolecular Substances, Molecular Sequence Data, Oncogene Proteins v-fos, Phosphorylation, Protein Biosynthesis, Proto-Oncogene Mas, Proto-Oncogene Proteins c-fos, Proto-Oncogene Proteins c-jun, Recombinant Proteins, Reticulocytes, Tetradecanoylphorbol Acetate, Transfection, Animals, Rabbits
Source:	Science
ISSN:	0036-8075
Publisher:	American Association for the Advancement of Science
Volume:	258
Number:	5090
Page Range:	1941-1944
Date:	18 December 1992
Official Publication:	https://doi.org/10.1126/science.1470918
PubMed:	View item in PubMed

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