beta-Arrestin-1 directly interacts with Gas and regulates its function | |
Li, B; Wang, CC; Zhou, ZC; Zhao, J; Pei, G | |
刊名 | FEBS LETTERS |
2013 | |
卷号 | 587期号:5页码:410-416 |
关键词 | beta-Arrestin-1 G protein Interaction Biolayer interferometry analysis GTP gamma S binding and release |
通讯作者 | Zhao, J (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, 320 Yue Yang Rd, Shanghai 200031, Peoples R China.,jzhao@sibs.ac.cn ; gpei@sibs.ac.cn |
英文摘要 | beta-Arrestins function to mediate G protein-coupled receptor (GPCR) desensitization and internalization and to initiate G protein independent signaling of GPCRs. Elucidating how beta-arrestin and G protein signal pathways coordinate with each other is important to fully understand GPCR signaling. Here we report that beta-arrestin-1 directly interacts with G alpha(s). Purified beta-arrestin-1 binds to G alpha(s) in a rapid association and dissociation manner. beta-Arrestin-1 promotes the binding and the release of GTP gamma S from G alpha(s) in vitro. beta-Arrestin-1 L33K mutant shows reduced interaction with G alpha(s) and has no detectable effects on G alpha(s) function. Our study thus reveals a direct crosstalk of beta-arrestin-1 with G alpha(s). Structured summary of protein interactions: G alpha q physically interacts with Beta-arrestin-1 by cross-linking study (View interaction). G alpha q physically interacts with Beta-arrestin-1 by anti tag coimmunoprecipitation (View interaction). G alpha s binds to Beta-arrestin-1 by biophysical (View Interaction: 1, 2). G alpha s physically interacts with Beta-arrestin-1 by anti tag coimmunoprecipitation (View interaction). Beta-arrestin-1 physically interacts with Gas by anti bait coimmunoprecipitation (View interaction). G alpha s physically interacts with Beta-arrestin-1 by cross-linking study (View interaction). (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
学科主题 | Biochemistry & Molecular Biology; Biophysics; Cell Biology |
类目[WOS] | Biochemistry & Molecular Biology ; Biophysics ; Cell Biology |
关键词[WOS] | NUCLEOTIDE EXCHANGE FACTOR ; HETEROTRIMERIC G-PROTEINS ; BETA-ARRESTIN ; BETA(2)-ADRENERGIC RECEPTOR ; CRYSTAL-STRUCTURE ; GTPASE ACTIVITY ; ALPHA-SUBUNITS ; ACTIVATION ; BINDING ; MECHANISM |
收录类别 | SCI |
语种 | 英语 |
WOS记录号 | WOS:000315217900005 |
内容类型 | 期刊论文 |
版本 | 出版稿 |
源URL | [http://202.127.25.143/handle/331003/392] |
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 | Li, B,Wang, CC,Zhou, ZC,et al. beta-Arrestin-1 directly interacts with Gas and regulates its function[J]. FEBS LETTERS,2013,587(5):410-416. |
APA | Li, B,Wang, CC,Zhou, ZC,Zhao, J,&Pei, G.(2013).beta-Arrestin-1 directly interacts with Gas and regulates its function.FEBS LETTERS,587(5),410-416. |
MLA | Li, B,et al."beta-Arrestin-1 directly interacts with Gas and regulates its function".FEBS LETTERS 587.5(2013):410-416. |
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