Abstract：
:Epilepsy is a common brain disorder throughout history. Epilepsy-related ligand-receptor complex, LGI1-ADAM22, regulates synaptic transmission and has emerged as a determinant of brain excitability, as their mutations and acquired LGI1 autoantibodies cause epileptic disorders in human. Here, we report the crystal structure of human LGI1-ADAM22 complex, revealing a 2:2 heterotetrameric assembly. The hydrophobic pocket of the C-terminal epitempin-repeat (EPTP) domain of LGI1 binds to the metalloprotease-like domain of ADAM22. The N-terminal leucine-rich repeat and EPTP domains of LGI1 mediate the intermolecular LGI1-LGI1 interaction. A pathogenic R474Q mutation of LGI1, which does not exceptionally affect either the secretion or the ADAM22 binding, is located in the LGI1-LGI1 interface and disrupts the higher-order assembly of the LGI1-ADAM22 complex in vitro and in a mouse model for familial epilepsy. These studies support the notion that the LGI1-ADAM22 complex functions as the trans-synaptic machinery for precise synaptic transmission.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Yamagata A,Miyazaki Y,Yokoi N,Shigematsu H,Sato Y,Goto-Ito S,Maeda A,Goto T,Sanbo M,Hirabayashi M,Shirouzu M,Fukata Y,Fukata M,Fukai Sdoi
10.1038/s41467-018-03947-wsubject
Has Abstractpub_date
2018-04-18 00:00:00pages
1546issue
1issn
2041-1723pii
10.1038/s41467-018-03947-wjournal_volume
9pub_type
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