Signal transduction within the nucleus by mitogen-activated protein kinase
Graduate School of Biomedical Sciences; Howard Hughes Medical Institute; Program in Molecular Medicine; Department of Biochemistry and Molecular Biology
Life Sciences | Medicine and Health Sciences
The nucleus is an important target of signal transduction by growth factor receptors that stimulate mitogen-activated protein (MAP) kinases. We tested the hypothesis that MAP kinases have a signaling role within the nucleus by examining the effect of the expression of a human MAP kinase isoform (p41mapk) in tissue culture cells. The expressed p41mapk was found to be localized in both the cytoplasmic and nuclear compartments of the cells. Significantly, the expression of p41mapk caused an increase in the phosphorylation of a nuclear substrate: Ser62 of c-Myc. Phosphorylation at Ser62 stimulated the activity of the NH2-terminal transactivation domain of c-Myc. Thus, p41mapk causes the phosphorylation and regulation of a physiologically significant nuclear target of signal transduction. These data establish that at least one MAP kinase isoform has a nuclear role during signal transduction.
J Biol Chem. 1992 Dec 5;267(34):24796-804.
The Journal of biological chemistry
Seth, Alpna; Gonzalez, Fernando A.; Gupta, Shashi; Raden, David L.; and Davis, Roger J., "Signal transduction within the nucleus by mitogen-activated protein kinase" (1992). GSBS Student Publications. 1098.