Lutterbach B, Hann S R
Department of Cell Biology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-2175, USA.
J Cell Biochem. 1999 Mar 15;72(4):483-91. 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.
我们已经分离并鉴定了与c-Myc反式激活结构域相关联并磷酸化Ser-62的细胞激酶。我们证明，细胞丝裂原活化蛋白激酶（Map激酶）在严格条件下与c-Myc相关联并磷酸化Ser-62。我们还发现，佛波酯（TPA）刺激与Myc相关的Map激酶的活性以磷酸化Ser-62。然而，在对细胞进行TPA处理后，我们未观察到内源性c-Myc中Ser-62磷酸化增加。由于与c-Myc相关的Map激酶的调节与c-Myc中Ser-62磷酸化的体内调节不相关，我们得出结论，Map激酶不是Ser-62的体内激酶。虽然Ser-62磷酸化不受TPA影响，但TPA显著上调了不同丝氨酸残基的磷酸化。
