标题:Structural Mechanism of the Arrestin-3/JNK3 Interaction
作者:Park, Ji Young; Qu, Chang-xiu; Li, Rui-rui; Yang, Fan; Yu, Xiao; Tian, Zhao-mei; Shen, Yue-mao; Cai, Bo-yang; Yun, Youngjoo; Sun, Ji 更多
作者机构:[Park, Ji Young; Yun, Youngjoo; Chung, Ka Young] Sungkyunkwan Univ, Sch Pharm, 2066 Seobu Ro, Suwon 16419, South Korea.; [Qu, Chang-xiu; Cai, Bo-yan 更多
通讯作者:Chung, KY;Sun, JP;Sun, JP;Sun, JP
通讯作者地址:[Chung, KY]Sungkyunkwan Univ, Sch Pharm, 2066 Seobu Ro, Suwon 16419, South Korea;[Sun, JP]Peking Univ, Key Lab Mol Cardiovasc Sci, Minist Educ, Dept P 更多
来源:STRUCTURE
出版年:2019
卷:27
期:7
页码:1162-+
DOI:10.1016/j.str.2019.04.002
摘要:Arrestins, in addition to desensitizing GPCR-induced G protein activation, also mediate G protein-independent signaling by interacting with various signaling proteins. Among these, arrestins regulate MAPK signal transduction by scaffolding mitogen-activated protein kinase (MAPK) signaling components such as MAPKKK, MAPKK, and MAPK. In this study, we investigated the binding mode and interfaces between arrestin-3 and JNK3 using hydrogen/deuterium exchange mass spectrometry, F-19-NMR, and tryptophan-induced Atto 655 fluorescence-quenching techniques. Results suggested that the beta 1 strand of arrestin-3 is the major and potentially only interaction site with JNK3. The results also suggested that C-lobe regions near the activation loop of JNK3 form the potential binding interface, which is variable depending on the ATP binding status. Because the beta 1 strand of arrestin-3 is buried by the C-terminal strand in its basal state, C-terminal truncation (i.e., pre-activation) of arrestin-3 facilitates the arrestin-3/JNK3 interaction.
收录类别:SCOPUS;SCIE
资源类型:期刊论文
原文链接:https://www.scopus.com/inward/record.uri?eid=2-s2.0-85067879481&doi=10.1016%2fj.str.2019.04.002&partnerID=40&md5=57d790a27a9ef862573e423f1dc022fa
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