Structural insights into modulation and selectivity of transsynaptic neurexin–LRRTM interaction

Atsushi Yamagata, Sakurako Goto-Ito, Yusuke Sato, Tomoko Shiroshima, Asami Maeda, Masahiko Watanabe, Takashi Saitoh, Katsumi Maenaka, Tohru Terada, Tomoyuki Yoshida, Takeshi Uemura () and Shuya Fukai ()
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Atsushi Yamagata: The University of Tokyo
Sakurako Goto-Ito: The University of Tokyo
Yusuke Sato: The University of Tokyo
Tomoko Shiroshima: The University of Tokyo
Asami Maeda: The University of Tokyo
Masahiko Watanabe: Hokkaido University Faculty of Medicine
Takashi Saitoh: Hokkaido University of Science
Katsumi Maenaka: Hokkaido University
Tohru Terada: The University of Tokyo
Tomoyuki Yoshida: University of Toyama
Takeshi Uemura: CREST, JST
Shuya Fukai: The University of Tokyo

Nature Communications, 2018, vol. 9, issue 1, 1-11

Abstract: Abstract Leucine-rich repeat transmembrane neuronal proteins (LRRTMs) function as postsynaptic organizers that induce excitatory synapses. Neurexins (Nrxns) and heparan sulfate proteoglycans have been identified as presynaptic ligands for LRRTMs. Specifically, LRRTM1 and LRRTM2 bind to the Nrxn splice variant lacking an insert at the splice site 4 (S4). Here, we report the crystal structure of the Nrxn1β–LRRTM2 complex at 3.4 Å resolution. The Nrxn1β–LRRTM2 interface involves Ca2+-mediated interactions and overlaps with the Nrxn–neuroligin interface. Together with structure-based mutational analyses at the molecular and cellular levels, the present structural analysis unveils the mechanism of selective binding between Nrxn and LRRTM1/2 and its modulation by the S4 insertion of Nrxn.

Date: 2018
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DOI: 10.1038/s41467-018-06333-8

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