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Structure of Slitrk2–PTPδ complex reveals mechanisms for splicing-dependent trans-synaptic adhesion

Selective binding between pre- and postsynaptic adhesion molecules can induce synaptic differentiation. Here we report the crystal structure of a synaptogenic trans-synaptic adhesion complex between Slit and Trk-like family member 2 (Slitrk2) and receptor protein tyrosine phosphatase (RPTP) δ. The s...

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Autores principales: Yamagata, Atsushi, Sato, Yusuke, Goto-Ito, Sakurako, Uemura, Takeshi, Maeda, Asami, Shiroshima, Tomoko, Yoshida, Tomoyuki, Fukai, Shuya
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4437028/
https://www.ncbi.nlm.nih.gov/pubmed/25989451
http://dx.doi.org/10.1038/srep09686
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author Yamagata, Atsushi
Sato, Yusuke
Goto-Ito, Sakurako
Uemura, Takeshi
Maeda, Asami
Shiroshima, Tomoko
Yoshida, Tomoyuki
Fukai, Shuya
author_facet Yamagata, Atsushi
Sato, Yusuke
Goto-Ito, Sakurako
Uemura, Takeshi
Maeda, Asami
Shiroshima, Tomoko
Yoshida, Tomoyuki
Fukai, Shuya
author_sort Yamagata, Atsushi
collection PubMed
description Selective binding between pre- and postsynaptic adhesion molecules can induce synaptic differentiation. Here we report the crystal structure of a synaptogenic trans-synaptic adhesion complex between Slit and Trk-like family member 2 (Slitrk2) and receptor protein tyrosine phosphatase (RPTP) δ. The structure and site-directed mutational analysis revealed the structural basis of splicing-dependent adhesion between Slitrks and type IIa RPTPs for inducing synaptic differentiation.
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spelling pubmed-44370282015-06-01 Structure of Slitrk2–PTPδ complex reveals mechanisms for splicing-dependent trans-synaptic adhesion Yamagata, Atsushi Sato, Yusuke Goto-Ito, Sakurako Uemura, Takeshi Maeda, Asami Shiroshima, Tomoko Yoshida, Tomoyuki Fukai, Shuya Sci Rep Article Selective binding between pre- and postsynaptic adhesion molecules can induce synaptic differentiation. Here we report the crystal structure of a synaptogenic trans-synaptic adhesion complex between Slit and Trk-like family member 2 (Slitrk2) and receptor protein tyrosine phosphatase (RPTP) δ. The structure and site-directed mutational analysis revealed the structural basis of splicing-dependent adhesion between Slitrks and type IIa RPTPs for inducing synaptic differentiation. Nature Publishing Group 2015-05-19 /pmc/articles/PMC4437028/ /pubmed/25989451 http://dx.doi.org/10.1038/srep09686 Text en Copyright © 2015, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder in order to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Yamagata, Atsushi
Sato, Yusuke
Goto-Ito, Sakurako
Uemura, Takeshi
Maeda, Asami
Shiroshima, Tomoko
Yoshida, Tomoyuki
Fukai, Shuya
Structure of Slitrk2–PTPδ complex reveals mechanisms for splicing-dependent trans-synaptic adhesion
title Structure of Slitrk2–PTPδ complex reveals mechanisms for splicing-dependent trans-synaptic adhesion
title_full Structure of Slitrk2–PTPδ complex reveals mechanisms for splicing-dependent trans-synaptic adhesion
title_fullStr Structure of Slitrk2–PTPδ complex reveals mechanisms for splicing-dependent trans-synaptic adhesion
title_full_unstemmed Structure of Slitrk2–PTPδ complex reveals mechanisms for splicing-dependent trans-synaptic adhesion
title_short Structure of Slitrk2–PTPδ complex reveals mechanisms for splicing-dependent trans-synaptic adhesion
title_sort structure of slitrk2–ptpδ complex reveals mechanisms for splicing-dependent trans-synaptic adhesion
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4437028/
https://www.ncbi.nlm.nih.gov/pubmed/25989451
http://dx.doi.org/10.1038/srep09686
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