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

✍ Scribed by Bart Lutterbach; Stephen R. Hann

• Publisher: John Wiley and Sons
• Year: 1999
• Tongue: English
• Weight: 114 KB
• Volume: 72
• Category: Article
• ISSN: 0730-2312
• DOI: 10.1002/(sici)1097-4644(19990315)72:4<483::aid-jcb4>3.0.co;2-i

✦ Synopsis

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.