Mechanisms of splicing-dependent trans-synaptic adhesion by PTPδ–IL1RAPL1/IL-1RAcP for synaptic differentiation

Atsushi Yamagata, Tomoyuki Yoshida (), Yusuke Sato, Sakurako Goto-Ito, Takeshi Uemura, Asami Maeda, Tomoko Shiroshima, Shiho Iwasawa-Okamoto, Hisashi Mori, Masayoshi Mishina and Shuya Fukai ()
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Atsushi Yamagata: Structural Biology Laboratory, Synchrotron Radiation Research Organization and Institute of Molecular and Cellular Biosciences, The University of Tokyo
Tomoyuki Yoshida: Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama
Yusuke Sato: Structural Biology Laboratory, Synchrotron Radiation Research Organization and Institute of Molecular and Cellular Biosciences, The University of Tokyo
Sakurako Goto-Ito: Structural Biology Laboratory, Synchrotron Radiation Research Organization and Institute of Molecular and Cellular Biosciences, The University of Tokyo
Takeshi Uemura: CREST, JST
Asami Maeda: Structural Biology Laboratory, Synchrotron Radiation Research Organization and Institute of Molecular and Cellular Biosciences, The University of Tokyo
Tomoko Shiroshima: Structural Biology Laboratory, Synchrotron Radiation Research Organization and Institute of Molecular and Cellular Biosciences, The University of Tokyo
Shiho Iwasawa-Okamoto: Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama
Hisashi Mori: Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama
Masayoshi Mishina: Graduate School of Medicine, The University of Tokyo
Shuya Fukai: Structural Biology Laboratory, Synchrotron Radiation Research Organization and Institute of Molecular and Cellular Biosciences, The University of Tokyo

Nature Communications, 2015, vol. 6, issue 1, 1-11

Abstract: Abstract Synapse formation is triggered through trans-synaptic interaction between pairs of pre- and postsynaptic adhesion molecules, the specificity of which depends on splice inserts known as ‘splice-insert signaling codes’. Receptor protein tyrosine phosphatase δ (PTPδ) can bidirectionally induce pre- and postsynaptic differentiation of neurons by trans-synaptically binding to interleukin-1 receptor accessory protein (IL-1RAcP) and IL-1RAcP-like-1 (IL1RAPL1) in a splicing-dependent manner. Here, we report crystal structures of PTPδ in complex with IL1RAPL1 and IL-1RAcP. The first immunoglobulin-like (Ig) domain of IL1RAPL1 directly recognizes the first splice insert, which is critical for binding to IL1RAPL1. The second splice insert functions as an adjustable linker that positions the Ig2 and Ig3 domains of PTPδ for simultaneously interacting with the Ig1 domain of IL1RAPL1 or IL-1RAcP. We further identified the IL1RAPL1-specific interaction, which appears coupled to the first-splice-insert-mediated interaction. Our results thus reveal the decoding mechanism of splice-insert signaling codes for synaptic differentiation induced by trans-synaptic adhesion between PTPδ and IL1RAPL1/IL-1RAcP.

Date: 2015
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DOI: 10.1038/ncomms7926

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