Fos-Associated Protein-P39 Is the Product of the Jun Proto-Oncogene

Rauscher, F. J., Cohen, D. R., Curran, T., Bos, T. J., Vogt, P. K., Bohmann, D., Tjian, R., Franza, B. R. (May 1988) Fos-Associated Protein-P39 Is the Product of the Jun Proto-Oncogene. Science, 240 (4855). pp. 1010-1016. ISSN 0036-8075

URL: http://www.ncbi.nlm.nih.gov/pubmed/3130660
DOI: 10.1126/science.3130660

Abstract

The Fos protein complex and several Fos-related antigens (FRA) bind specifically to a sequence element referred to as the HeLa cell activator protein 1 (AP-1) binding site. A combination of structural and immunological comparisons has identified the Fos-associated protein (p39) as the protein product of the jun proto-oncogene (c-Jun). The p39/Jun protein is one of the major polypeptides identified in AP-1 oligonucleotide affinity chromatography extracts of cellular proteins. These preparations of AP-1 also contain Fos and several FRA's. Some of these proteins bind to the AP-1 site directly whereas others, like Fos, appear to bind indirectly via protein-protein interactions. Cell-surface stimulation results in an increase in c-fos and c-jun products. Thus, the products of two protooncogenes (and several related proteins), induced by extracellular stimuli, form a complex that associates with transcriptional control elements containing AP-1 sites, thereby potentially mediating the long-term responses to signals that regulate growth control and development.

Item Type: Paper
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
organs, tissues, organelles, cell types and functions > cell types and functions > cell functions
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > DNA binding protein
CSHL Authors:
Communities: CSHL labs
Depositing User: Gail Sherman
Date: 20 May 1988
Date Deposited: 19 Sep 2017 19:23
Last Modified: 19 Sep 2017 19:23
Related URLs:
URI: https://repository.cshl.edu/id/eprint/35201

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