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Signal transduction within the nucleus by mitogen-activated protein kinase
A Seth1, F A Gonzalez, S Gupta
1Howard Hughes Medical Institute, University of Massachusetts Medical School, Worcester 01605.
The Journal of Biological Chemistry
|December 5, 1992
Summary
Mitogen-activated protein (MAP) kinases signal within the cell nucleus. This study shows that MAP kinase p41mapk phosphorylates c-Myc, regulating its activity and confirming a nuclear role for MAP kinases in signal transduction.
Area of Science:
- Cell biology
- Molecular biology
- Signal transduction
Background:
- Growth factor receptors activate mitogen-activated protein (MAP) kinases, which are crucial in cellular signaling.
- The nucleus is a key cellular compartment targeted by signal transduction pathways.
Purpose of the Study:
- To investigate the hypothesis that MAP kinases play a signaling role within the nucleus.
- To examine the nuclear localization and function of a specific human MAP kinase isoform, p41mapk.
Main Methods:
- Expression of human MAP kinase isoform (p41mapk) in tissue culture cells.
- Analysis of p41mapk localization within cytoplasmic and nuclear compartments.
- Assessment of the effect of p41mapk expression on the phosphorylation of nuclear substrates, specifically c-Myc.
Main Results:
- Expressed p41mapk was detected in both the cytoplasm and nucleus.
- p41mapk expression led to increased phosphorylation of c-Myc at Ser62.
- Phosphorylation at Ser62 enhanced the activity of the NH2-terminal transactivation domain of c-Myc.
Conclusions:
- MAP kinase p41mapk directly phosphorylates and regulates the nuclear protein c-Myc.
- These findings establish a nuclear signaling role for at least one MAP kinase isoform in response to growth factor receptor stimulation.
- MAP kinases are involved in nuclear signal transduction pathways, impacting gene regulation via targets like c-Myc.
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