Structure of BAI1/ELMO2 complex reveals an action mechanism of adhesion GPCRs via ELMO family scaffolds

Zhuangfeng Weng, Chenghao Situ, Lin Lin, Zhenguo Wu, Jinwei Zhu () and Rongguang Zhang ()
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Zhuangfeng Weng: University of Chinese Academy of Sciences
Chenghao Situ: Hong Kong University of Science and Technology, Kowloon
Lin Lin: University of Chinese Academy of Sciences
Zhenguo Wu: Hong Kong University of Science and Technology, Kowloon
Jinwei Zhu: University of Chinese Academy of Sciences
Rongguang Zhang: University of Chinese Academy of Sciences

Nature Communications, 2019, vol. 10, issue 1, 1-10

Abstract: 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 BAI1 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.

Date: 2019
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DOI: 10.1038/s41467-018-07938-9

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