Review - Regulation of G protein-coupled receptor signaling by A-kinase anchoring proteins

被引:22
作者
Appert-Collin, Aline [1 ]
Baisamy, Laurent [1 ]
Diviani, Dario [1 ]
机构
[1] Fac Med, Dept Pharmacol & Toxicol, CH-1005 Lausanne, Switzerland
关键词
A-kinase anchoring protein; G protein-coupled receptor; Rho-GTPase; signal transduction;
D O I
10.1080/10799890600923211
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
Specificity of transduction events is controlled at the molecular level by scaffold, anchoring, and adaptor proteins, which position signaling enzymes at proper subcellular localization. This allows their efficient catalytic activation and accurate substrate selection. A-kinase anchoring proteins (AYAPs) are group of functionally related proteins that compartmentalize the cAMP-dependent protein kinase (PKA) and other signaling enyzmes at precise subcellular sites in close proximity to their physiological substrate(s) and favor specific phosphorylation events. Recent evidence suggests that AKAP transduction complexes play a key role in regulating G protein-coupled receptor (GPCR) signaling. Regulation can occur at multiple levels because AKAPs have been shown both to directly modulate GPCR function and to act as downstream effectors of GPCR signaling. In this minireview, we focus on the molecular mechanisms through which AKAP-signaling complexes modulate GPCR transduction cascades.
引用
收藏
页码:631 / 646
页数:16
相关论文
共 58 条
[41]   Gravin, an autoantigen recognized by serum from myasthenia gravis patients, is a kinase scaffold protein [J].
Nauert, JB ;
Klauck, TM ;
Langeberg, LK ;
Scott, JD .
CURRENT BIOLOGY, 1997, 7 (01) :52-62
[42]  
Newlon MG, 1999, NAT STRUCT BIOL, V6, P222
[43]   The A-kinase anchoring domain of type II alpha cAMP-dependent protein kinase is highly helical [J].
Newlon, MG ;
Roy, M ;
Hausken, ZE ;
Scott, JD ;
Jennings, PA .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (38) :23637-23644
[44]   Interaction of heterotrimeric G13 protein with an A-kinase-anchoring protein 110 (AKAP110) mediates cAMP-independent PKA activation [J].
Niu, JX ;
Vaiskunaite, R ;
Suzuki, N ;
Kozasa, T ;
Carr, DW ;
Dulin, N ;
Voyno-Yasenetskaya, TA .
CURRENT BIOLOGY, 2001, 11 (21) :1686-1690
[45]   Imaging kinase-AKAP79-phosphatase scaffold complexes at the plasma membrane in living cells using FRET microscopy [J].
Oliveria, SF ;
Gomez, LL ;
Dell'Acqua, ML .
JOURNAL OF CELL BIOLOGY, 2003, 160 (01) :101-112
[46]   The role of Rho in G protein-coupled receptor signal transduction [J].
Sah, VP ;
Seasholtz, TM ;
Sagi, SA ;
Brown, JH .
ANNUAL REVIEW OF PHARMACOLOGY AND TOXICOLOGY, 2000, 40 :459-489
[47]  
SCOTT JD, 1992, NEWS PHYSIOL SCI, V7, P143
[48]   CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN-KINASES [J].
SCOTT, JD .
PHARMACOLOGY & THERAPEUTICS, 1991, 50 (01) :123-145
[49]   Dynamic complexes of β2-adrenergic receptors with protein kinases and phosphatases and the role of gravin [J].
Shih, ML ;
Lin, FB ;
Scott, JD ;
Wang, HY ;
Malbon, CC .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (03) :1588-1595
[50]   Protein kinase A regulates AKAP250 (gravin) scaffold binding to the β2-adrenergic receptor [J].
Tao, JC ;
Wang, HY ;
Malbon, CC .
EMBO JOURNAL, 2003, 22 (24) :6419-6429