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 and consequent stabilization of the
protein. These results illustrate the relevance of regulated protein degradation in the signal-
dependent control of gene expression.
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.
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.
AAAS