Insulin activates a PD 098059‐sensitive kinase that is involved in the regulation of p70S6K and PHAS‐I

FEBS Letters

Scott, Pamela H¹  Lawrence, John C¹ 

[1] Department of Pharmacology, University of Virginia School of Medicine, 1300 Jefferson Park Avenue, Charlottesville, VA 22908, USA

关键词: Insulin;    p70S6K;    PD 098059;    MAP kinase kinase;    PHAS-I;   

DOI  :  10.1016/S0014-5793(97)00500-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Incubating either Chinese hamster ovary (CHO) cells or 3T3-L1 adipocytes with insulin increased the phosphorylation of the eIF-4E-binding protein, PHAS-I. Insulin also activated p70^S6K and the Erk-1 and Erk-2 isoforms of mitogen-activated protein kinase (MAP kinase). However, the concentrations of the hormone needed to activate MAP kinase were 10–100 times higher than those needed to increase PHAS-I phosphorylation and p70^S6K activity. Incubating cells with the inhibitor of MAP kinase kinase (MEK) activation, PD 098059, blocked the effects of low concentrations of insulin on PHAS-I and p70^S6K. The effects of the inhibitor were overcome by increasing concentrations of insulin. The results indicate that insulin activates a PD 098059-sensitive kinase that is involved in the regulation of both p70^S6K and PHAS-I.

【 授权许可】

Unknown