Protein kinases, from B to C

被引：28

作者：

Cameron, A. J.

De Rycker, M.

Calleja, V.

Alcor, D.

Kjaer, S.

Kostelecky, B.

Saurin, A.

Faisal, A.

Laguerre, M.

Hemmings, B. A.

McDonald, N.

Larijani, B.

Parker, P. J.

机构：

[1] London Res Inst, Prot Phosphorylat Lab, London WC2A 3PX, England

[2] London Res Inst, Cell Biophys Lab, London WC2A 3PX, England

[3] London Res Inst, Struct Biol Lab, London WC2A 3PX, England

[4] European Chim Biol, Pessac, France

[5] Friedrich Miescher Inst Biomed Res, CH-4058 Basel, Switzerland

[6] Guys Hosp, Sect Canc Cell Biol & Imaging, Head Div Canc Studies KCL, London SE1 1UL, England

来源：

BIOCHEMICAL SOCIETY TRANSACTIONS | 2007年 / 35卷

关键词：

protein kinase B (PKB); protein kinase C (PKC); phosphomositide-dependent kinase 1 (PDK1); phosphorylation; pleckstrin homology domain (PH domain); protein serine/threonine kinase;

D O I：

10.1042/BST0351013

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 PKB (protein kinase B) and PKC (protein kinase C) families display highly related catalytic domains that require a largely conserved series of phosphorylations for the expression of their optimum activities. However, in cells, the dynamics of these modifications are quite distinct. Based on experimental evidence, it is argued that the underlying mechanisms determining these divergent behaviours relate to the very different manner in which their variant regulatory domains interact with their respective catalytic domains. it is concluded that the distinct behaviours of PKB and PKC proteins are defined by the typical ground states of these proteins.

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页码：1013 / 1017

页数：5

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