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Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors

文献类型:期刊论文

作者Zhou, X. Edward9,10; He, Yuanzheng9; de Waal, Parker W.9; Gao, Xiang9; Kang, Yanyong9; Van Eps, Ned11; Yin, Yanting9,10; Pal, Kuntal9; Goswami, Devrishi12; White, Thomas A.13
刊名CELL
出版日期2017-07-27
卷号170期号:3页码:457-+
ISSN号0092-8674
DOI10.1016/j.cell.2017.07.002
文献子类Article
英文摘要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.
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
资助项目NIH[DK071662] ; NIH[R01 GM108635] ; NIH[RO1 EY011500] ; NIH[R35 GM122491] ; NIH[RO1 EY005216] ; American Asthma Foundation[00000000] ; Jay and Betty Van Andel Foundation[00000000] ; Ministry of Science and Technology (China)[2012ZX09301001] ; Ministry of Science and Technology (China)[2012CB910403] ; Ministry of Science and Technology (China)[2013CB910600] ; Ministry of Science and Technology (China)[XDB08020303] ; Ministry of Science and Technology (China)[2013ZX09507001] ; Canada Excellence Research Chairs program[00000000] ; Canadian Institute for Advanced Research[00000000] ; Anne and Max Tanenbaum Chair in Neuroscience[00000000] ; Jules Stein Professorship Endowment[00000000] ; David Van Andel Advanced Electron Microscopy Core Facility[00000000] ; NSF Science and Technology Center[1231306]
WOS研究方向Biochemistry & Molecular Biology ; Cell Biology
语种英语
出版者CELL PRESS
WOS记录号WOS:000406462400006
源URL[http://119.78.100.183/handle/2S10ELR8/272557]  
专题药物靶标结构与功能中心
通讯作者Xu, H. Eric
作者单位1.Stanford Univ, Biophys Program, Stanford, CA 94305 USA;
2.Ctr Ultrafast Imaging, D-22761 Hamburg, Germany;
3.Univ Calif Los Angeles, Jules Stein Eye Inst, Los Angeles, CA 90095 USA;
4.Univ Calif Los Angeles, Dept Chem & Biochem, Los Angeles, CA 90095 USA;
5.Univ Southern Calif, Bridge Inst, Dept Chem, Los Angeles, CA 90089 USA;
6.ShanghaiTech Univ, iHuman Inst, 2F Bldg 6,99 Haike Rd, Shanghai 201210, Peoples R China;
7.Vanderbilt Univ, Dept Pharmacol, Nashville, TN 37232 USA;
8.Univ Toronto, Dept Mol Genet, Toronto, ON M5S 1A8, Canada
9.Van Andel Res Inst, Ctr Struct Biol & Drug Discovery, Lab Struct Sci, Grand Rapids, MI 49503 USA;
10.Chinese Acad Sci, Shanghai Inst Mat Med, Key Lab Receptor Res, VARI SIMM Ctr,Ctr Struct & Funct Drug Targets, Shanghai 201203, Peoples R China;
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-+.

入库方式: OAI收割

来源:上海药物研究所

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