cAMP effector mechanisms. Novel twists for an 'old' signaling system

被引：167

作者：

Kopperud, R ^{[1
]}

Krakstad, C ^{[1
]}

Selheim, F ^{[1
]}

Doskeland, SO ^{[1
]}

机构：

[1] Univ Bergen, Dept Anat & Cell Biol, N-5009 Bergen, Norway

来源：

FEBS LETTERS | 2003年 / 546卷 / 01期

关键词：

protein kinase A; cAMP-dependent protein kinase; cyclic AMP; Epac; extracellular signal-regulated kinase; Rap1; Rap2; guanine exchange factor;

D O I：

10.1016/S0014-5793(03)00563-5

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：

Cyclic AMP (cAMP) has traditionally been thought to act exclusively through cAMP-dependent protein kinase (cAPK, PKA), but a growing number of cAMP effects are not attributable to general activation of cAPK. At present, cAMP is known also to directly regulate ion channels and the ubiquitous Rap guanine exchange factors Epac 1 and 2. Adding to the sophistication of cAMP signaling is the fact that (1) the cAPK holoenzyme is incompletely dissociated even at saturating cAMP, the level of free R subunit of cAPK being able to regulate the maximal activity of cAPK, (2) cAPK activity can be modulated by oxidative glutathionylation, and (3) cAPK is anchored close to relevant substrates, other signaling enzymes, and local compartments of cAMP. Finally, we will demonstrate an example of fine-tuning of cAMP signaling through synergistic induction of neurite extensions by cAPK and Epac. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：121 / 126

页数：6

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