Involvement of the C-terminal proline-rich motif of G protein-coupled receptor kinases in recognition of activated rhodopsin

	Involvement of the C-terminal proline-rich motif of G protein-coupled receptor kinases in recognition of activated rhodopsin
	Gan, XQ; Ma, ZH; Deng, N; Wang, JY; Ding, JP; Li, L
刊名	JOURNAL OF BIOLOGICAL CHEMISTRY
	2004
卷号	279 期号:48 页码:49741-49746
通讯作者	Li, L (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, Mol Cell Biol Lab, Shanghai 200031, Peoples R China.,lli@sibs.ac.cn
英文摘要	G protein-coupled receptor kinases (GRKs) are a family of serine/threonine kinases that phosphorylate many activated G protein-coupled receptors (GPCRs) and play an important role in GPCR desensitization. Our previous work has demonstrated that the C-terminal conserved region (CC) of GRK-2 participates in interaction with rhodopsin and that this interaction is necessary for GRK-2-mediated receptor phosphorylation (Gan, X. Q., Wang, J. Y., Yang, Q. H., Li, Z., Liu, F., Pei, G., and Li, L. (2000) J. Biol. Chem. 275, 8469-8474). In this report, we further investigated whether the CC of other GRKs had the same functions and defined the specific sequences in CC that are required for the functions. The CC regions of GRK-1, GRK-2, and GRK-5, representatives of the three subfamilies of GRKs, could bind rhodopsin in vitro and inhibit GRK-2-mediated phosphorylation of rhodopsin, but not a peptide GRK substrate. Through a series of mutagenesis analyses, a proline-rich motif in the CC was identified as the key element involved in the interaction between the CC region and rhodopsin. Point mutations of this motif not only disrupted the interaction of GRK-2 with rhodopsin but also abolished the ability of GRK-2 to phosphorylate rhodopsin. The findings that the CC region of GRKs interact only with the light-activated but not the non-activated rhodopsin and that the N-terminal domain of GRK-2 interacts with rhodopsin in a light-independent manner suggest that the CC region is responsible for the recognition of activated GPCRs in the canonical model.
学科主题	Biochemistry & Molecular Biology
类目[WOS]	Biochemistry & Molecular Biology
关键词[WOS]	2 GRK2 ; PHOSPHORYLATES TUBULIN ; ESCHERICHIA-COLI ; BETA-GAMMA ; BINDING ; DOMAIN ; MECHANISM ; SUBUNITS ; MEMBRANE
收录类别	SCI
语种	英语
WOS记录号	WOS:000225229500025
内容类型	期刊论文
版本	出版稿
源URL	[http://202.127.25.143/handle/331003/2191]
专题	上海生化细胞研究所_上海生科院生化细胞研究所
推荐引用方式 GB/T 7714	Gan, XQ,Ma, ZH,Deng, N,et al. Involvement of the C-terminal proline-rich motif of G protein-coupled receptor kinases in recognition of activated rhodopsin[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2004,279(48):49741-49746.
APA	Gan, XQ,Ma, ZH,Deng, N,Wang, JY,Ding, JP,&Li, L.(2004).Involvement of the C-terminal proline-rich motif of G protein-coupled receptor kinases in recognition of activated rhodopsin.JOURNAL OF BIOLOGICAL CHEMISTRY,279(48),49741-49746.
MLA	Gan, XQ,et al."Involvement of the C-terminal proline-rich motif of G protein-coupled receptor kinases in recognition of activated rhodopsin".JOURNAL OF BIOLOGICAL CHEMISTRY 279.48(2004):49741-49746.