The mechanism of protein kinase regulation by protein phosphatases

被引：9

作者：

Barford, D ^{[1
]}

机构：

[1] Inst Canc Res, Chester Beatty Labs, Sect Struct Biol, London SW3 6JB, England

来源：

BIOCHEMICAL SOCIETY TRANSACTIONS | 2001年 / 29卷

关键词：

dual specificity protein phosphatases (DSPs); insulin receptor; insulin receptor kinase (IRK); kinase-associated phosphatase (KAP); phosphoproteins; protein tyrosine phosphatase IB; (PTP IB);

D O I：

10.1042/BST0290385

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Protein kinases are an important class of substrate of the protein phosphatases. We have examined the mechanism of dephosphorylation of the activation segments of the insulin receptor kinase and cyclin-dependent kinase 2 by their respective phosphatases, namely the tyrosine specific phosphatase PTP1B and the dual specificity phosphatase KAP. These studies reveal that PTP1B and KAP utilize contrasting mechanisms in order to dephosphorylate their substrates specifically.

引用

页码：385 / 391

页数：7

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