GSBS Student Publications

Title

Signal transduction within the nucleus by mitogen-activated protein kinase

UMMS Affiliation

Graduate School of Biomedical Sciences; Howard Hughes Medical Institute; Program in Molecular Medicine; Department of Biochemistry and Molecular Biology

Date

12-5-1992

Document Type

Article

Medical Subject Headings

Amino Acid Sequence; Animals; Blotting, Western; Calcium-Calmodulin-Dependent Protein Kinases; Cell Line; Cell Nucleus; Fluorescent Antibody Technique; Humans; Isoenzymes; Molecular Sequence Data; Peptides; Phosphopeptides; Phosphoproteins; Phosphorylation; Plasmids; Protein Kinases; Proto-Oncogene Proteins c-myc; Serine; *Signal Transduction; Substrate Specificity; Transfection

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

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.

Rights and Permissions

Citation: J Biol Chem. 1992 Dec 5;267(34):24796-804.

Related Resources

Link to Article in PubMed

Journal Title

The Journal of biological chemistry

PubMed ID

1332967