KESTREL: a powerful method for identifying the physiological substrates of protein kinases

被引：63

作者：

Cohen, P

Knebel, A

机构：

[1] MSI WTB Complex, MRC Prot Phosphorylat Unit, Dundee DD1 5EH, Scotland

[2] MSI WTB Complex, Kinasource Ltd, Dundee DD1 5EH, Scotland

来源：

BIOCHEMICAL JOURNAL | 2006年 / 393卷

基金：

英国医学研究理事会;

关键词：

glycogen synthase kinase 3 (GSK3); kinase substrate tracking and elucidation (KESTREL); mitogen-activated-protein-kinase-activated protein kinase-2 (MAPKAP-K2); protein kinase B (PKB); serum- and glucocorticoid-induced protein kinase (SGK);

D O I：

10.1042/BJ20051545

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：

The identification of all the substrates of every protein kinase is one of the major challenges of post-genomic research. Here we review a powerful method for tackling this problem that we have developed over the last 5 years. The method has so far been used to identify novel substrates for eight different protein kinases, demonstrating that it is of general utility. Importantly, the method can be used to identify distinct physiological substrates of protein kinases, such as PKB (protein kinase 13) and SGK (serum- and glucocorticoid-induced kinase), that are closely related in structure and have similar specificity determinants.

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页码：1 / 6

页数：6

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