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Intramolecular signal transduction in c-Jun
A G Papavassiliou1, M Treier, D Bohmann
1European Molecular Biology Laboratory, Differentiation Program, Heidelberg, Germany.
The EMBO Journal
|May 1, 1995
Summary
c-Jun DNA-binding is regulated by phosphorylation. Phorbol ester activation involves NH2-terminal phosphorylation, indirectly causing COOH-terminal dephosphorylation and altering DNA-binding site accessibility.
Area of Science:
- Molecular Biology
- Cell Signaling
- Transcription Factor Regulation
Background:
- c-Jun protein's DNA-binding activity is crucial for gene regulation.
- This activity is modulated by the phosphorylation status of specific residues near its COOH-terminus.
Purpose of the Study:
- To investigate the molecular events triggering c-Jun activation via dephosphorylation.
- To elucidate the role of phorbol esters in modulating c-Jun's DNA-binding potential.
Main Methods:
- Analysis of c-Jun phosphorylation and dephosphorylation events.
- Investigating signaling pathways initiated by phorbol esters.
Main Results:
- Phorbol ester treatment leads to indirect COOH-terminal dephosphorylation of c-Jun.
- This dephosphorylation is a consequence of an NH2-terminal phosphorylation event.
- Activation of DNA-binding involves altered accessibility of COOH-terminal phosphoacceptor sites.
Conclusions:
- c-Jun activation is indirectly regulated by NH2-terminal phosphorylation.
- The kinase/phosphatase system's direct regulation of COOH-terminal sites may not be the primary activation mechanism.
- Changes in phosphoacceptor site accessibility are key to c-Jun's DNA-binding activation.