Reduced Ubiquitin-Dependent Degradation of c-Jun After Phosphorylation by MAP Kinases

The proto-oncogene-encoded transcription factor c-Jun activates genes in response to a number of inducers that act through mitogen-activated protein kinase (MAPK) signal transduction pathways. The activation of c-Jun after phosphorylation by MAPK is accompanied by a reduction in c-Jun ubiquitination...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1997-01, Vol.275 (5298), p.400-402
Main Authors: Musti, Anna Maria, Treier, Mathias, Bohmann, Dirk
Format: Article
Language:English
Subjects:
3T3 Cells
Animals
Biological and medical sciences
Calcium-Calmodulin-Dependent Protein Kinases - metabolism
cdc42 GTP-Binding Protein, Saccharomyces cerevisiae
Cell Cycle Proteins - metabolism
Cell physiology
Cells
Fundamental and applied biological sciences. Psychology
Gels
Gene Expression Regulation
Genetic regulation
Genetic transcription
GTP-Binding Proteins - metabolism
Half lives
JNK Mitogen-Activated Protein Kinases
Mice
Mitogen-Activated Protein Kinases
Molecular and cellular biology
Molecular biology
NIH 3T3 cells
Phosphorylation
Physiological aspects
Proteins
Proto-Oncogene Proteins c-jun - metabolism
Radioactive decay
Regulation
Research Design
Signal Transduction
Transcription (Genetics)
Transfection
Ubiquitin
Ubiquitins
Ubiquitins - metabolism
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Summary:The proto-oncogene-encoded transcription factor c-Jun activates genes in response to a number of inducers that act through mitogen-activated protein kinase (MAPK) signal transduction pathways. The activation of c-Jun after phosphorylation by MAPK is accompanied by a reduction in c-Jun ubiquitination and consequent stabilization of the protein. These results illustrate the relevance of regulated protein degradation in the signal-dependent control of gene expression.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.275.5298.400