Arrestin times for compartmentalised cAMP signalling and phosphodiesterase-4 enzymes

被引:105
作者
Baillie, GS [1 ]
Houslay, MD [1 ]
机构
[1] Univ Glasgow, Inst Biomed & Life Sci, Div Biochem & Mol Biol, Mol Pharmacol Grp, Glasgow G12 8QQ, Lanark, Scotland
基金
英国医学研究理事会;
关键词
D O I
10.1016/j.ceb.2005.01.003
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Various methods reveal that cyclic AMP (cAMP) signalling in cells is compartmentalised. These methods use FRET probes based upon either protein kinase A (PKA) or EPAC, cAMP-gated ion channels, or the selective activation of AKAP-anchored PKA isoforms. The basis of compartmentalisation involves point sources of cAMP generation within sub-domains of the plasma membrane coupled to degradation by spatially segregated, anchored forms of cAMP phosphodiesterases. cAMP-specific phosphodiesterase-4 (PDE4) isoforms play a central role in determining compartmentalisation, as exemplified in cardiac myocytes; and T cells. The PKA phosphorylation status of the beta(2)-adrenoreceptor, and hence its ability to switch its signalling from G(s) to G(i) and thus to activate ERK, is regulated dynamically by the agonist-stimulated recruitment of PDE4 to the receptor in complex with P-arrestin. The co-receptor CD28 enhances signalling through the T-cell receptor by recruiting a PDE4/beta-arrestin complex, which then attenuates PKA phosphorylation of Csk.
引用
收藏
页码:129 / 134
页数:6
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