Structure of BAl1/ELMO2 complex reveals an action mechanism of adhesion GPCRs via ELMO family scaffolds
Weng, Zhuangfeng1,2,3; Situ, Chenghao4; Lin, Lin1,2; Wu, Zhenguo4; Zhu, Jinwei1,2; Zhang, Rongguang1,2,3
2019-01-03
Source PublicationNATURE COMMUNICATIONS
ISSN2041-1723
Volume10
Status已发表
DOI10.1038/s41467-018-07938-9
AbstractThe brain-specific angiogenesis inhibitor (BAI) subfamily of adhesion G protein-coupled receptors (aGPCRs) plays crucial roles in diverse cellular processes including phagocytosis, myoblast fusion, and synaptic development through the ELMO/DOCK/Rac signaling pathway, although the underlying molecular mechanism is not well understood. Here, we demonstrate that an evolutionarily conserved fragment located in the C-terminal cytoplasmic tail of BAI-aGPCRs is specifically recognized by the RBD-ARR-ELMO (RAE) supramodule of the ELMO family scaffolds. The crystal structures of ELMO2-RAE and its complex with BAH uncover the molecular basis of BAI/ELMO interactions. Based on the complex structure we identify aGPCR-GPR128 as another upstream receptor for the ELMO family scaffolds, most likely with a recognition mode similar to that of BAI/ELMO interactions. Finally, we map disease-causing mutations of BAI and ELMO and analyze their effects on complex formation.
Indexed BySCI
Language英语
Funding ProjectNational Natural Science Foundation of China[31770779] ; National Natural Science Foundation of China[U1532121] ; National Natural Science Foundation of China[31470733]
WOS Research AreaScience & Technology - Other Topics
WOS SubjectMultidisciplinary Sciences
WOS IDWOS:000454757900002
PublisherNATURE PUBLISHING GROUP
WOS KeywordBRAIN ANGIOGENESIS INHIBITOR-1 ; PROTEIN-COUPLED RECEPTORS ; BAI1 ; SYNAPTOGENESIS ; ENGULFMENT ; BINDING ; SYSTEM ; MODEL ; RAC1 ; GENE
Original Document TypeArticle
Citation statistics
Cited Times:10[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttps://kms.shanghaitech.edu.cn/handle/2MSLDSTB/30059
Collection生命科学与技术学院_博士生
生命科学与技术学院_特聘教授组_张荣光组
Corresponding AuthorZhu, Jinwei; Zhang, Rongguang
Affiliation1.Chinese Acad Sci, Shanghai Inst Biochem & Cell Biol, CAS Ctr Excellence Mol Cell Sci, State Key Lab Mol Biol, 333 Haike Rd, Shanghai 201210, Peoples R China
2.Univ Chinese Acad Sci, Shanghai Sci Res Ctr, 333 Haike Rd, Shanghai 201210, Peoples R China
3.ShanghaiTech Univ, Sch Life Sci & Technol, 100 Haike Rd, Shanghai 201210, Peoples R China
4.Hong Kong Univ Sci & Technol, State Key Lab Neurosci, Ctr Syst Biol & Human Hlth, Div Life Sci,Ctr Stem Cell Res,Kowloon, Hong Kong, Peoples R China
First Author AffilicationSchool of Life Science and Technology
Corresponding Author AffilicationSchool of Life Science and Technology
Recommended Citation
GB/T 7714
Weng, Zhuangfeng,Situ, Chenghao,Lin, Lin,et al. Structure of BAl1/ELMO2 complex reveals an action mechanism of adhesion GPCRs via ELMO family scaffolds[J]. NATURE COMMUNICATIONS,2019,10.
APA Weng, Zhuangfeng,Situ, Chenghao,Lin, Lin,Wu, Zhenguo,Zhu, Jinwei,&Zhang, Rongguang.(2019).Structure of BAl1/ELMO2 complex reveals an action mechanism of adhesion GPCRs via ELMO family scaffolds.NATURE COMMUNICATIONS,10.
MLA Weng, Zhuangfeng,et al."Structure of BAl1/ELMO2 complex reveals an action mechanism of adhesion GPCRs via ELMO family scaffolds".NATURE COMMUNICATIONS 10(2019).
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