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| Structure of BAl1/ELMO2 complex reveals an action mechanism of adhesion GPCRs via ELMO family scaffolds | |
| 2019-01-03 | |
| Source Publication | NATURE COMMUNICATIONS
 |
| ISSN | 2041-1723 |
| Volume | 10 |
| Status | 已发表 |
| DOI | 10.1038/s41467-018-07938-9 |
| Abstract | 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. |
| Indexed By | SCI ; SCIE |
| Language | 英语 |
| Funding Project | National Natural Science Foundation of China[31770779] ; National Natural Science Foundation of China[U1532121] ; National Natural Science Foundation of China[31470733] |
| WOS Research Area | Science & Technology - Other Topics |
| WOS Subject | Multidisciplinary Sciences |
| WOS ID | WOS:000454757900002 |
| Publisher | NATURE PUBLISHING GROUP |
| WOS Keyword | BRAIN ANGIOGENESIS INHIBITOR-1 ; PROTEIN-COUPLED RECEPTORS ; BAI1 ; SYNAPTOGENESIS ; ENGULFMENT ; BINDING ; SYSTEM ; MODEL ; RAC1 ; GENE |
| Original Document Type | Article |
| Citation statistics | |
| Document Type | 期刊论文 |
| Identifier | https://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 Author | Zhu, Jinwei; Zhang, Rongguang |
| Affiliation | 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 |
| First Author Affilication | School of Life Science and Technology |
| Corresponding Author Affilication | School 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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