Fos is phosphorylated by p34cdc2, cAMP-dependent protein kinase and protein kinase C at multiple sites clustered within regulatory regions.

Abate, C., Marshak, D. R., Curran, T. (December 1991) Fos is phosphorylated by p34cdc2, cAMP-dependent protein kinase and protein kinase C at multiple sites clustered within regulatory regions. Oncogene, 6 (12). pp. 2179-2185. ISSN 0950-9232

Abstract

The proto-oncogene c-fos encodes a nuclear protein (Fos) that functions in transcriptional regulation in response to extracellular signals. Fos is extensively modified in the nucleus by serine and threonine phosphorylation. It has been suggested that phosphorylation may play an important role in regulating Fos function in normal and transformed cells. As a first step in addressing this issue, we have used purified Fos as a substrate for several serine-threonine protein kinases, including cAMP-dependent protein kinase (PKA), protein kinase C (PKC) and p34cdc2. Each of these kinases phosphorylated Fos at several unique sites. These sites were located within two regions that were previously shown to reduce the transcriptional activity of Fos in vitro. Several of the sites modified in vitro were also shown to be phosphorylated in serum-stimulated fibroblasts. These findings demonstrate that Fos is a target for several protein kinases involved in signal transduction and suggest that phosphorylation could regulate the transcriptional properties of Fos.

Item Type:	Paper
Uncontrolled Keywords:	DNA-BINDING DOMAINS OSTEO-SARCOMA VIRUS LEUCINE ZIPPER JUN TRANSCRIPTION IDENTIFICATION ACTIVATION ONCOGENE INVITRO SERUM
Subjects:	bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > cdc2 bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > transcription factor > Cyclic AMP bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase > Protein kinase C
CSHL Authors:	Marshak, Daniel R.
Communities:	CSHL labs
Depositing User:	Matt Covey
Date:	December 1991
Date Deposited:	11 Jan 2016 17:55
Last Modified:	11 Jan 2016 17:55
URI:	https://repository.cshl.edu/id/eprint/32077

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