Structure of BAl1/ELMO2 complex reveals an action mechanism of adhesion GPCRs via ELMO family scaffolds

doi:10.1038/s41467-018-07938-9

	Structure of BAl1/ELMO2 complex reveals an action mechanism of adhesion GPCRs via ELMO family scaffolds
	Weng, Zhuangfeng1,2,3 ; Situ, Chenghao 4; Lin, Lin 1,2; Wu, Zhenguo 4; Zhu, Jinwei 1,2; Zhang, Rongguang1,2,3
	2019-01-03
发表期刊	NATURE COMMUNICATIONS
ISSN	2041-1723
卷号	10
发表状态	已发表
DOI	10.1038/s41467-018-07938-9
摘要	The 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.
收录类别	SCI ; SCIE
语种	英语
资助项目	National Natural Science Foundation of China[31770779] ; National Natural Science Foundation of China[U1532121] ; National Natural Science Foundation of China[31470733]
WOS研究方向	Science & Technology - Other Topics
WOS类目	Multidisciplinary Sciences
WOS记录号	WOS:000454757900002
出版者	NATURE PUBLISHING GROUP
WOS关键词	BRAIN ANGIOGENESIS INHIBITOR-1 ; PROTEIN-COUPLED RECEPTORS ; BAI1 ; SYNAPTOGENESIS ; ENGULFMENT ; BINDING ; SYSTEM ; MODEL ; RAC1 ; GENE
原始文献类型	Article
引用统计
文献类型	期刊论文
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/30059
专题	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
通讯作者	Zhu, Jinwei; Zhang, Rongguang
作者单位	1.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
第一作者单位	生命科学与技术学院
通讯作者单位	生命科学与技术学院
推荐引用方式 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).