Structural basis of trans-synaptic interactions between PTPδ and SALMs for inducing synapse formation

Sakurako Goto-Ito, Atsushi Yamagata, Yusuke Sato, Takeshi Uemura, Tomoko Shiroshima, Asami Maeda, Ayako Imai, Hisashi Mori, Tomoyuki Yoshida () and Shuya Fukai ()
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Sakurako Goto-Ito: The University of Tokyo
Atsushi Yamagata: The University of Tokyo
Yusuke Sato: The University of Tokyo
Takeshi Uemura: CREST, JST
Tomoko Shiroshima: The University of Tokyo
Asami Maeda: The University of Tokyo
Ayako Imai: Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama
Hisashi Mori: Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama
Tomoyuki Yoshida: Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama
Shuya Fukai: The University of Tokyo

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

Abstract: Abstract Synapse formation is triggered by trans-synaptic interactions of cell adhesion molecules, termed synaptic organizers. Three members of type-II receptor protein tyrosine phosphatases (classified as type-IIa RPTPs; PTPδ, PTPσ and LAR) are known as presynaptic organizers. Synaptic adhesion-like molecules (SALMs) have recently emerged as a family of postsynaptic organizers. Although all five SALM isoforms can bind to the type-IIa RPTPs, only SALM3 and SALM5 reportedly have synaptogenic activities depending on their binding. Here, we report the crystal structures of apo-SALM5, and PTPδ–SALM2 and PTPδ–SALM5 complexes. The leucine-rich repeat (LRR) domains of SALMs interact with the second immunoglobulin-like (Ig) domain of PTPδ, whereas the Ig domains of SALMs interact with both the second and third Ig domains of PTPδ. Unexpectedly, the structures exhibit the LRR-mediated 2:2 complex. Our synaptogenic co-culture assay using site-directed SALM5 mutants demonstrates that presynaptic differentiation induced by PTPδ–SALM5 requires the dimeric property of SALM5.

Date: 2018
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DOI: 10.1038/s41467-017-02417-z

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