Dimerization and DNA-Binding Alter Phosphorylation of Fos and Jun

Abate, C., Baker, S. J., Lees-Miller, S. P., Anderson, C. W., Marshak, D. R., Curran, T. (July 1993) Dimerization and DNA-Binding Alter Phosphorylation of Fos and Jun. Proc Natl Acad Sci U S A, 90 (14). pp. 6766-6770. ISSN 0027-8424

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URL: http://www.ncbi.nlm.nih.gov/pubmed/8341696

Abstract

Fos and Jun form dimeric complexes that bind to activator protein 1 (AP-1) DNA sequences and regulate gene expression. The levels of expression and activities of these proteins are regulated by a variety of extracellular stimuli. They are thought to function in nuclear signal transduction processes in many different cell types. The role of Fos and Jun in gene transcription is complex and may be regulated in several ways including association with different dimerization partners, interactions with other transcription factors, effects on DNA topology, and reduction/oxidation of a conserved cysteine residue in the DNA-binding domain. In addition, phosphorylation has been suggested to control the activity of Fos and Jun. Here we show that phosphorylation of Fos and Jun by several protein kinases is affected by dimerization and binding to DNA. Jun homodimers are phosphorylated efficiently by casein kinase II, whereas Fos-Jun heterodimers are not. DNA binding also reduces phosphorylation of Jun by casein kinase II, p34cdc2 (cdc2) kinase, and protein kinase C. Phosphorylation of Fos by cAMP-dependent protein kinase and cdc2 is relatively insensitive to dimerization and DNA binding, whereas phosphorylation of Fos and Jun by DNA-dependent protein kinase is dramatically stimulated by binding to the AP-1 site. These results imply that different protein kinases can distinguish among Fos and Jun proteins in the form of monomers, homodimers, and heterodimers and between DNA-bound and non-DNA-bound proteins. Thus, potentially, these different states of Fos and Jun can be recognized and regulated independently by phosphorylation.

Item Type: Paper
Uncontrolled Keywords: TRANSCRIPTION FACTORS ONCOGENESIS SIGNAL TRANSDUCTION POSTTRANSLATIONAL MODIFICATION ACTIVATED PROTEIN-KINASE LEUCINE ZIPPER C-JUN MOUSE FIBROBLASTS INVITRO EXPRESSION DOMAINS HETERODIMERS TRANSITION COMMON
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 > DNA, RNA structure, function, modification > genes, structure and function > genes: types > c-jun
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > DNA binding protein
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > genes: types > oncogene
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression > phosphorylation
CSHL Authors:
Communities: CSHL labs
Depositing User: Matt Covey
Date: 15 July 1993
Date Deposited: 07 Apr 2016 18:24
Last Modified: 09 Nov 2017 19:59
PMCID: PMC47013
Related URLs:
URI: http://repository.cshl.edu/id/eprint/32594

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