Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors
2017-07-27
发表期刊CELL (IF:45.5[JCR-2023],49.0[5-Year])
ISSN0092-8674
卷号170期号:3页码:457-+
发表状态已发表
DOI10.1016/j.cell.2017.07.002
摘要G protein-coupled receptors (GPCRs) mediate diverse signaling in part through interaction with arrestins, whose binding promotes receptor internalization and signaling through G protein-independent pathways. High-affinity arrestin binding requires receptor phosphorylation, often at the receptor's C-terminal tail. Here, we report an X-ray free electron laser (XFEL) crystal structure of the rhodopsin-arrestin complex, in which the phosphorylated C terminus of rhodopsin forms an extended intermolecular b sheet with the N-terminal b strands of arrestin. Phosphorylation was detected at rhodopsin C-terminal tail residues T336 and S338. These two phosphoresidues, together with E341, form an extensive network of electrostatic interactions with three positively charged pockets in arrestin in a mode that resembles binding of the phosphorylated vasopressin-2 receptor tail to beta-arrestin-1. Based on these observations, we derived and validated a set of phosphorylation codes that serve as a common mechanism for phosphorylation-dependent recruitment of arrestins by GPCRs.
收录类别SCI
语种英语
资助项目NSF Science and Technology Center[1231306]
WOS研究方向Biochemistry & Molecular Biology ; Cell Biology
WOS类目Biochemistry & Molecular Biology ; Cell Biology
WOS记录号WOS:000406462400006
出版者CELL PRESS
WOS关键词BETA-ARRESTIN ; BETA(2)-ADRENERGIC RECEPTOR ; MOLECULAR-DYNAMICS ; CRYSTAL-STRUCTURE ; 7-TRANSMEMBRANE RECEPTORS ; VISUAL ARRESTIN ; DOWN-REGULATION ; C-TERMINUS ; MECHANISM ; BINDING
原始文献类型Article
通讯作者Xu, H. Eric
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文献类型期刊论文
条目标识符https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/2882
专题iHuman研究所
iHuman研究所_特聘教授组_Raymond Stevens组
通讯作者Xu, H. Eric
作者单位
1.Chinese Acad Sci, Shanghai Inst Mat Med, Key Lab Receptor Res, VARI SIMM Ctr,Ctr Struct & Funct Drug Targets, Shanghai 201203, Peoples R China
2.Van Andel Res Inst, Ctr Struct Biol & Drug Discovery, Lab Struct Sci, Grand Rapids, MI 49503 USA
3.Univ Toronto, Dept Biochem, Toronto, ON M5S 1A8, Canada
4.Scripps Florida, Scripps Res Inst, Dept Mol Med, Jupiter, FL 33458 USA
5.Deutsch Elekt Synchrotron DESY, Ctr Free Electron Laser Sci, D-22607 Hamburg, Germany
6.Stanford Univ, Dept Comp Sci, Stanford, CA 94305 USA
7.Stanford Univ, Dept Mol & Cellular Physiol, Stanford, CA 94305 USA
8.Stanford Univ, Dept Struct Biol, Stanford, CA 94305 USA
9.Stanford Univ, Inst Computat & Math Engn, Stanford, CA 94305 USA
10.Stanford Univ, Biophys Program, Stanford, CA 94305 USA
11.Ctr Ultrafast Imaging, D-22761 Hamburg, Germany
12.Univ Calif Los Angeles, Jules Stein Eye Inst, Los Angeles, CA 90095 USA
13.Univ Calif Los Angeles, Dept Chem & Biochem, Los Angeles, CA 90095 USA
14.Univ Southern Calif, Bridge Inst, Dept Chem, Los Angeles, CA 90089 USA
15.ShanghaiTech Univ, iHuman Inst, 2F Bldg 6,99 Haike Rd, Shanghai 201210, Peoples R China
16.Vanderbilt Univ, Dept Pharmacol, Nashville, TN 37232 USA
17.Univ Toronto, Dept Mol Genet, Toronto, ON M5S 1A8, Canada
推荐引用方式
GB/T 7714
Zhou, X. Edward,He, Yuanzheng,de Waal, Parker W.,et al. Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors[J]. CELL,2017,170(3):457-+.
APA Zhou, X. Edward.,He, Yuanzheng.,de Waal, Parker W..,Gao, Xiang.,Kang, Yanyong.,...&Xu, H. Eric.(2017).Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors.CELL,170(3),457-+.
MLA Zhou, X. Edward,et al."Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors".CELL 170.3(2017):457-+.
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