Identification of a Nerve Growth Factor-Regulated and Epidermal Growth Factor-Regulated Protein-Kinase That Phosphorylates the Protooncogene Product C-Fos

Taylor, L. K., Marshak, D. R., Landreth, G. E. (January 1993) Identification of a Nerve Growth Factor-Regulated and Epidermal Growth Factor-Regulated Protein-Kinase That Phosphorylates the Protooncogene Product C-Fos. Proc Natl Acad Sci U S A, 90 (2). pp. 368-372. ISSN 0027-8424

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Abstract

Nerve growth factor (NGF) treatment of rat pheochromocytoma (PC12) cells induces the synthesis of the transcription factor c-Fos, which becomes highly phosphorylated relative to that produced as a result of depolarization of the cell. A peptide derived from the carboxyl terminus of c-Fos (residues 359-370, RKGSSSNEPSSD) containing putative phosphorylation sites was used to detect a NGF-stimulated Fos kinase. NGF treatment of PC12 cells resulted in a rapid activation of a protein kinase which phosphorylated both the c-Fos peptide and authentic c-Fos at its carboxyl terminus. The kinase was selectively activated by NGF and epidermal growth factor but was not induced by depolarization or other agents. The c-Fos peptide was phosphorylated at a serine corresponding to Ser362, a site critically implicated in the capacity of c-Fos to exhibit transrepressive activity [Ofir, R., Dwarki, V. J., Rashid, D. & Verma, I. M. (1990) Nature (London) 348, 80-82)]. The NGF-stimulated Fos kinase may play an important role in regulating the expression and transforming potential of c-Fos.

Item Type:	Paper
Uncontrolled Keywords:	TRANSCRIPTIONAL REGULATION TRANSREPRESSION PC12 CELLS SERUM RESPONSE ELEMENT DNA-BINDING ACTIVITY PC12 CELLS GENE-EXPRESSION TRANSCRIPTIONAL ACTIVATION ONCOGENE FOS JUN AP-1 INDUCTION PROMOTER
Subjects:	bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > genes: types > c-fos bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > epidermal growth factor bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > fibroblast growth factor bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > genes: types > oncogene
CSHL Authors:	Marshak, Daniel R.
Communities:	CSHL labs
Depositing User:	Matt Covey
Date:	15 January 1993
Date Deposited:	07 Apr 2016 19:27
Last Modified:	09 Nov 2017 20:04
PMCID:	PMC45663
Related URLs:	Publisher
URI:	https://repository.cshl.edu/id/eprint/32596

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