β肾上腺素能受体激酶
化学
差速器(机械装置)
受体
生物物理学
药理学
生物
物理
G蛋白偶联受体
生物化学
热力学
作者
Antonietta Picascia,Loredana Capobianco,Luisa Iacovelli,Antonio De Blasi
出处
期刊:Methods in Enzymology
日期:2004-01-01
卷期号:: 337-353
被引量:10
标识
DOI:10.1016/s0076-6879(04)90021-3
摘要
G-protein-coupled receptor kinases (GRK) contain a regulator of G-protein signaling (RGS)-like domain located at the N terminus (GRK-Nter) of their sequence. This domain is present in all the GRK subtypes, but the RGS-like domain of GRK2 was documented to be functionally active, as it is able to interact selectively with Galphaq (both in vitro and in cells) and to inhibit Galphaq-dependent signaling. In contrast GRK4, GRK5, and GRK6 are unable to interact with Galphaq. This article describes the methodology to investigate the modulatory activity of GRK2 and GRK4 on GPCR-stimulated Galphaq signaling. This analysis is essentially based on three types of experiments: (a) study of the effect of the GRK-Nter on GPCR-dependent signaling; (b) analysis of the binding of GRK-Nter to Galphaq in vitro; and (c) analysis of the interaction of GRK with Galphaq in cells.
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