REGULATION OF PROTEIN SERINE-THREONINE PHOSPHATASE TYPE-2A BY TYROSINE PHOSPHORYLATION

被引：562

作者：

CHEN, J ^{[1
]}

MARTIN, BL ^{[1
]}

BRAUTIGAN, DL ^{[1
]}

机构：

[1] BROWN UNIV, DIV BIOL & MED, BIOCHEM SECT, PROVIDENCE, RI 02912 USA

来源：

SCIENCE | 1992年 / 257卷 / 5074期

关键词：

D O I：

10.1126/science.1325671

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Extracellular signals that promote cell growth activate cascades of protein kinases. The kinases are dephosphorylated and deactivated by a single type-2A protein phosphatase. The catalytic subunit of type-2A protein phosphatase was phosphorylated by tyrosine-specific protein kinases. Phosphorylation was enhanced in the presence of the phosphatase inhibitor okadaic acid, consistent with an autodephosphorylation reaction. More than 90% of the activity of phosphatase 2A was lost when thioadenosine triphosphate was used to produce a thiophosphorylated protein resistant to autodephosphorylation. Phosphorylation in vitro occurred exclusively on Tyr307. Phosphorylation was catalyzed by p60v-src, p56lck, epidermal growth factor receptors, and insulin receptors. Transient deactivation of phosphatase 2A might enhance transmission of cellular signals through kinase cascades within cells.

引用

页码：1261 / 1264

页数：4

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