GSBS Student Publications

Title

A phosphorylation site located in the NH2-terminal domain of c-Myc increases transactivation of gene expression

UMMS Affiliation

Graduate School of Biomedical Sciences; Program in Molecular Medicine

Date

12-15-1991

Document Type

Article

Medical Subject Headings

Amino Acid Sequence; Animals; CHO Cells; Chloramphenicol O-Acetyltransferase; Cricetinae; Gene Expression; Gene Expression Regulation; Hela Cells; Humans; Mutagenesis, Insertional; Phosphorylation; Plasmids; Proto-Oncogene Proteins c-myc; *Trans-Activation (Genetics); Transcription, Genetic; Transfection

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

The c-myc gene encodes a sequence-specific DNA-binding protein (c-Myc) that forms leucine zipper complexes and can act as a transcription factor. Growth factor stimulation of cells causes the phosphorylation of the c-Myc transcriptional activation domain at Ser62 within a proline-rich region that is highly conserved among members of the Myc family (Alvarez, E., Northwood, I.C., Gonzalez, F. A., Latour, D. A., Seth, A., Abate, C., Curran, T., and Davis, R. J. (1991) J. Biol. Chem. 266, 15277-15285). This phosphorylation site is a substrate for growth factor-regulated MAP kinases and for the cell cycle-dependent protein kinase p34cdc2. We report that serum treatment of cells results in a marked increase in the transactivation of gene expression mediated by the c-Myc transcriptional activation domain. A point mutation at the site of growth factor-stimulated phosphorylation (Ser62) decreases the serum induction of transactivation. These data indicate that the c-Myc transcriptional activation domain may be a direct target of signal transduction pathways.

Rights and Permissions

Citation: J Biol Chem. 1991 Dec 15;266(35):23521-4.

Related Resources

Link to Article in PubMed

Journal Title

The Journal of biological chemistry

PubMed ID

1748630