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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Chen, R. H. Abate, C. Blenis, J. |
| Description | Author Affiliation: Chen RH ( Department of Cell Biology, Harvard Medical School, Boston, MA 02115.); |
| Abstract | Phosphorylation of the C terminus of c-Fos has been implicated in serum response element-mediated repression of c-fos transcription after its induction by serum growth factors. The growth-regulated enzymes responsible for this phosphorylation in early G1 phase of the cell cycle and the sites of phosphorylation have not been identified. We now provide evidence that two growth-regulated, nucleus- and cytoplasm-localized protein kinases, 90-kDa ribosomal S6 kinase (RSK) and mitogen-activated protein kinase (MAP kinase), contribute to the serum-induced phosphorylation of c-Fos. The major phosphopeptides derived from biosynthetically labeled c-Fos correspond to phosphopeptides generated after phosphorylation of c-Fos in vitro with both RSK and MAP kinase. The phosphorylation sites identified for RSK (Ser-362) and MAP kinase (Ser-374) are in the transrepression domain. Cooperative phosphorylation at these sites by both enzymes was observed in vitro and reflected in vivo by the predominance of the peptide phosphorylated on both sites, as opposed to singly phosphorylated peptides. This study suggests a role for nuclear RSK and MAP kinase in modulating newly synthesized c-Fos phosphorylation and downstream signaling. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 23 |
| Volume Number | 90 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1993-01-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Calcium-Calmodulin-Dependent Protein Kinases Metabolism Genes, Fos Protein-Serine-Threonine Kinases Proto-Oncogene Proteins C-fos 3T3 Cells Amino Acid Sequence Animals Gene Expression Regulation In Vitro Techniques Mice Molecular Sequence Data Mutagenesis, Site-Directed Peptide Mapping Phosphoserine RNA, Messenger Genetics Recombinant Proteins Ribosomal Protein S6 Kinases Sequence Deletion Structure-Activity Relationship Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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