The nuts and bolts of AGC protein kinases

被引：1007

作者：

Pearce, Laura R. ^{[1
]}

Komander, David ^{[2
]}

Alessi, Dario R. ^{[1
]}

机构：

[1] Univ Dundee, Coll Life Sci, Phosphorylat Unit, Dundee DD1 5EH, Scotland

[2] MRC, Div Prot & Nucle Acid Chem, Mol Biol Lab, Cambridge CB2 0QH, England

来源：

NATURE REVIEWS MOLECULAR CELL BIOLOGY | 2010年 / 11卷 / 01期

基金：

英国医学研究理事会;

关键词：

HYDROPHOBIC MOTIF PHOSPHORYLATION; RHO-ASSOCIATED KINASE; CATALYTIC DOMAIN; MYOTONIC-DYSTROPHY; CRYSTAL-STRUCTURE; DOCKING SITE; PHOSPHOINOSITIDE; 3-KINASE; SUBSTRATE-SPECIFICITY; FEEDBACK INHIBITION; PDK1; ACTIVATION;

D O I：

10.1038/nrm2822

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The AGC kinase subfamily of protein kinases contains 60 members, including PKA, PKG and PKC. The family comprises some intensely examined protein kinases (such as Akt, S6K, RSK, MSK, PDK1 and GRK) as well as many less well-studied enzymes (such as SGK, NDR, LATS, CRIK, SGK494, PRKX, PRKY and MAST). Research has shed new light onto the architecture and regulatory mechanisms of these kinases. In addition, AGC kinases mediate diverse and important cellular functions, and their mutation and/or dysregulation contributes to the pathogenesis of many human diseases, including cancer and diabetes.

引用

页码：9 / 22

页数：14

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