PDZ-domain arrays for identifying components of GPCR signaling complexes

被引:5
作者
Day, Peter [1 ]
Kobilka, Brian [1 ]
机构
[1] Stanford Univ, Sch Med, Dept Mol & Cellular Physiol, Stanford, CA 94305 USA
关键词
D O I
10.1016/j.tips.2006.08.003
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
Many G-protein-coupled receptors (GPCRs) modulate the activity of multiple effectors. Yet, despite this apparent promiscuity, signaling in the context of differentiated cells is often highly specific. This specificity is attributable to the formation of cell-type-specific signaling complexes that are held together by scaffolding proteins, many of which contain one or more PDZ domains. Identifying the set of potential interactions among GPCRs, other signaling molecules and these scaffolding proteins is essential for understanding physiological signaling processes. A recent article describes an elegantly simple PDZ-domain array that can identify potential interacting partners of GPCRs and other signaling molecules.
引用
收藏
页码:509 / 511
页数:3
相关论文
共 15 条
[1]   GPCR interacting proteins (GIP) [J].
Bockaert, J ;
Fagni, L ;
Dumuis, A ;
Marin, P .
PHARMACOLOGY & THERAPEUTICS, 2004, 103 (03) :203-221
[2]   The β2-adrenergic receptor delivers an antiapoptotic signal to cardiac myocytes through Gi-dependent coupling to phosphatidylinositol 3′-kinase [J].
Chesley, A ;
Lundberg, MS ;
Asai, T ;
Xiao, RP ;
Ohtani, S ;
Lakatta, EG ;
Crow, MT .
CIRCULATION RESEARCH, 2000, 87 (12) :1172-1179
[3]  
Devic E, 2001, MOL PHARMACOL, V60, P577
[4]   P2Y1 receptor signaling is controlled by interaction with the PDZ scaffold NHERF-2 [J].
Fam, SR ;
Paquet, M ;
Castleberry, AM ;
Oller, H ;
Lee, CJ ;
Traynelis, SF ;
Smith, Y ;
Yun, CC ;
Hall, RA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2005, 102 (22) :8042-8047
[5]   Proteomic analysis of β1-adrenergic receptor interactions with PDZ scaffold proteins [J].
He, JQ ;
Bellini, M ;
Inuzuka, H ;
Xu, JG ;
Xiong, Y ;
Yang, XM ;
Castleberry, AM ;
Hall, RA .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (05) :2820-2827
[6]   Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex [J].
Hillier, BJ ;
Christopherson, KS ;
Prehoda, KE ;
Bredt, DS ;
Lim, WA .
SCIENCE, 1999, 284 (5415) :812-815
[7]   β1-adrenergic receptor association with PSD-95 -: Inhibition of receptor internalization and facilitation of β1-adrenergic receptor interaction with N-methyl-D-aspartate receptors [J].
Hu, LYA ;
Tang, YT ;
Miller, WE ;
Cong, M ;
Lau, AG ;
Lefkowitz, RJ ;
Hall, RA .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (49) :38659-38666
[8]   Convergent signal transduction pathways controlling cardiomyocyte survival and function: the role of PI 3-kinase and Akt [J].
Matsui, T ;
Rosenzweig, A .
JOURNAL OF MOLECULAR AND CELLULAR CARDIOLOGY, 2005, 38 (01) :63-71
[9]  
Nourry Claire, 2003, Sci STKE, V2003, pRE7
[10]   Uncovering quantitative protein interaction networks for mouse PDZ domains using protein microarrays [J].
Stiffler, MA ;
Grantcharova, VP ;
Sevecka, M ;
MacBeath, G .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2006, 128 (17) :5913-5922