, a bio/informatics shared resource is still "open for business" - Visit the CDS website

c-Myc transactivation domain-associated kinases: questionable role for map kinases in c-Myc phosphorylation.

Lutterbach B, Hann SR
J Cell Biochem. 1999 72 (4): 483-91

PMID: 10022608 · DOI:10.1002/(sici)1097-4644(19990315)72:4<483::aid-jcb4>3.0.co;2-i

We have isolated and characterized cellular kinases which associate with the transactivation domain of c-Myc and phosphorylate Ser-62. We demonstrate that cellular Map kinases associate with c-Myc under stringent conditions and phosphorylate Ser-62. We also find that TPA stimulates the activity of the Myc-associated Map kinase to phosphorylate Ser-62. However, we do not observe an increase in Ser-62 phosphorylation in endogenous c-Myc after TPA treatment of cells. Since the regulation of the c-Myc-associated Map kinases does not correlate with the in vivo regulation of Ser-62 phosphorylation in c-Myc, we conclude that Map kinases are not the in vivo kinases for Ser-62. Although Ser-62 phosphorylation was not affected by TPA, phosphorylation at a different serine residue was significantly upregulated by TPA.

MeSH Terms (11)

3T3 Cells Animals Calcium-Calmodulin-Dependent Protein Kinases COS Cells Mice Phosphopeptides Phosphorylation Phosphoserine Protein Kinases Proto-Oncogene Proteins c-myc Tetradecanoylphorbol Acetate

Connections (1)

This publication is referenced by other Labnodes entities: