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

Author

Listed:
  • Sakurako Goto-Ito

    (The University of Tokyo
    The University of Tokyo
    CREST, JST)

  • Atsushi Yamagata

    (The University of Tokyo
    The University of Tokyo
    CREST, JST
    Graduate School of Frontier Sciences, The University of Tokyo)

  • Yusuke Sato

    (The University of Tokyo
    The University of Tokyo
    CREST, JST
    Graduate School of Frontier Sciences, The University of Tokyo)

  • Takeshi Uemura

    (CREST, JST
    Shinshu University School of Medicine
    Institute for Biomedical Sciences, Interdisciplinary Cluster for Cutting Edge Research, Shinshu University)

  • Tomoko Shiroshima

    (The University of Tokyo
    The University of Tokyo
    CREST, JST)

  • Asami Maeda

    (The University of Tokyo
    The University of Tokyo
    CREST, JST)

  • 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
    PRESTO, JST)

  • Shuya Fukai

    (The University of Tokyo
    The University of Tokyo
    CREST, JST
    Graduate School of Frontier Sciences, The University of Tokyo)

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.

Suggested Citation

  • Sakurako Goto-Ito & Atsushi Yamagata & Yusuke Sato & Takeshi Uemura & Tomoko Shiroshima & Asami Maeda & Ayako Imai & Hisashi Mori & Tomoyuki Yoshida & Shuya Fukai, 2018. "Structural basis of trans-synaptic interactions between PTPδ and SALMs for inducing synapse formation," Nature Communications, Nature, vol. 9(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-017-02417-z
    DOI: 10.1038/s41467-017-02417-z
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