AKAP79 and the evolution of the AKAP model

被引：110

作者：

Dodge, K ^{[1
]}

Scott, JD ^{[1
]}

机构：

[1] Oregon Hlth Sci Univ, Vollum Inst, Howard Hughes Med Inst, Portland, OR 97201 USA

来源：

FEBS LETTERS | 2000年 / 476卷 / 1-2期

关键词：

D O I：

10.1016/S0014-5793(00)01671-9

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：

A molecular explanation for the specificity of the cAMP-dependent protein kinase (PKA) can be provided by its compartmentalization through association with A-kinase-anchoring proteins (AKAPs), Structural and functional studies have led to the development of an anchoring model proposing that AKAPs contain a common PKA binding domain and a unique subcellular targeting domain. The discovery that AKAPs can bind other signaling enzymes led to the addition of a third property, that of scaffolding molecule. Recent research has now expanded the role of AKAPs to members of multiunit complexes containing both upstream activators and downstream targets. (C) 2000 Federation of European Biochemical Societies, Published by Elsevier Science B.V. All rights reserved.

引用

页码：58 / 61

页数：4

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