Protease‐activated kinase II as the mediator of epidermal growth factor‐stimulated phosphorylation of ribosomal protein S6

FEBS Letters

Perisic, Olga¹  Traugh, Jolinda A.¹ 

[1] Department of Biochemistry, University of California, Riverside, CA 92521, USA

关键词: Protein kinase;    Epidermal growth factor;    Phosphorylation;    Ribosome;    Protease-activated kinase;    Swiss 3T3 cell;    EGF;    epidermal growth factor;    TPA;    12-O-tetradecanoyl phorbol-13-acetate;    PAK II;    protease activated kinase II;   

DOI  :  10.1016/0014-5793(85)80779-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Epidermal growth factor stimulates phosphorylation of ribosomal protein S6 in serum-starved Swiss 3T3 cells, leading to the formation of highly phosphorylated derivatives containing 4–5 phosphates. Two-dimensional analysis of tryptic phosphopeptides of S6 shows an identical pattern to the ones obtained previously in other cells in response to insulin and the tumor promoting phorbol ester, 12-O-tetradecanoyl phorbol-13-acetate. This suggests a common intracellular mediator of S6 phosphorylation by different growth promoting agents. It is proposed that the potential mediator of this phosphorylation is the Ca²⁺-independent, cAMP-independent protein kinase, protease activated kinase II, as shown by the extent of phosphorylation and the tryptic phosphopeptide maps of S6 with highly purified enzyme [(1983) J. Biol. Chem. 258, 13998-14002].

【 授权许可】

Unknown