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Crystal structures of the TRIC trimeric intracellular cation channel orthologues
Ca(2+) release from the sarcoplasmic reticulum (SR) and endoplasmic reticulum (ER) is crucial for muscle contraction, cell growth, apoptosis, learning and memory. The trimeric intracellular cation (TRIC) channels were recently identified as cation channels balancing the SR and ER membrane potentials...
Autores principales: | , , , , , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5143425/ https://www.ncbi.nlm.nih.gov/pubmed/27909292 http://dx.doi.org/10.1038/cr.2016.140 |
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author | Kasuya, Go Hiraizumi, Masahiro Maturana, Andrés D Kumazaki, Kaoru Fujiwara, Yuichiro Liu, Keihong Nakada-Nakura, Yoshiko Iwata, So Tsukada, Keisuke Komori, Tomotaka Uemura, Sotaro Goto, Yuhei Nakane, Takanori Takemoto, Mizuki Kato, Hideaki E Yamashita, Keitaro Wada, Miki Ito, Koichi Ishitani, Ryuichiro Hattori, Motoyuki Nureki, Osamu |
author_facet | Kasuya, Go Hiraizumi, Masahiro Maturana, Andrés D Kumazaki, Kaoru Fujiwara, Yuichiro Liu, Keihong Nakada-Nakura, Yoshiko Iwata, So Tsukada, Keisuke Komori, Tomotaka Uemura, Sotaro Goto, Yuhei Nakane, Takanori Takemoto, Mizuki Kato, Hideaki E Yamashita, Keitaro Wada, Miki Ito, Koichi Ishitani, Ryuichiro Hattori, Motoyuki Nureki, Osamu |
author_sort | Kasuya, Go |
collection | PubMed |
description | Ca(2+) release from the sarcoplasmic reticulum (SR) and endoplasmic reticulum (ER) is crucial for muscle contraction, cell growth, apoptosis, learning and memory. The trimeric intracellular cation (TRIC) channels were recently identified as cation channels balancing the SR and ER membrane potentials, and are implicated in Ca(2+) signaling and homeostasis. Here we present the crystal structures of prokaryotic TRIC channels in the closed state and structure-based functional analyses of prokaryotic and eukaryotic TRIC channels. Each trimer subunit consists of seven transmembrane (TM) helices with two inverted repeated regions. The electrophysiological, biochemical and biophysical analyses revealed that TRIC channels possess an ion-conducting pore within each subunit, and that the trimer formation contributes to the stability of the protein. The symmetrically related TM2 and TM5 helices are kinked at the conserved glycine clusters, and these kinks are important for the channel activity. Furthermore, the kinks of the TM2 and TM5 helices generate lateral fenestrations at each subunit interface. Unexpectedly, these lateral fenestrations are occupied with lipid molecules. This study provides the structural and functional framework for the molecular mechanism of this ion channel superfamily. |
format | Online Article Text |
id | pubmed-5143425 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-51434252016-12-23 Crystal structures of the TRIC trimeric intracellular cation channel orthologues Kasuya, Go Hiraizumi, Masahiro Maturana, Andrés D Kumazaki, Kaoru Fujiwara, Yuichiro Liu, Keihong Nakada-Nakura, Yoshiko Iwata, So Tsukada, Keisuke Komori, Tomotaka Uemura, Sotaro Goto, Yuhei Nakane, Takanori Takemoto, Mizuki Kato, Hideaki E Yamashita, Keitaro Wada, Miki Ito, Koichi Ishitani, Ryuichiro Hattori, Motoyuki Nureki, Osamu Cell Res Original Article Ca(2+) release from the sarcoplasmic reticulum (SR) and endoplasmic reticulum (ER) is crucial for muscle contraction, cell growth, apoptosis, learning and memory. The trimeric intracellular cation (TRIC) channels were recently identified as cation channels balancing the SR and ER membrane potentials, and are implicated in Ca(2+) signaling and homeostasis. Here we present the crystal structures of prokaryotic TRIC channels in the closed state and structure-based functional analyses of prokaryotic and eukaryotic TRIC channels. Each trimer subunit consists of seven transmembrane (TM) helices with two inverted repeated regions. The electrophysiological, biochemical and biophysical analyses revealed that TRIC channels possess an ion-conducting pore within each subunit, and that the trimer formation contributes to the stability of the protein. The symmetrically related TM2 and TM5 helices are kinked at the conserved glycine clusters, and these kinks are important for the channel activity. Furthermore, the kinks of the TM2 and TM5 helices generate lateral fenestrations at each subunit interface. Unexpectedly, these lateral fenestrations are occupied with lipid molecules. This study provides the structural and functional framework for the molecular mechanism of this ion channel superfamily. Nature Publishing Group 2016-12 2016-12-02 /pmc/articles/PMC5143425/ /pubmed/27909292 http://dx.doi.org/10.1038/cr.2016.140 Text en Copyright © 2016 Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences http://creativecommons.org/licenses/by-nc-nd/4.0/ This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 4.0 Unported 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 to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/4.0/ |
spellingShingle | Original Article Kasuya, Go Hiraizumi, Masahiro Maturana, Andrés D Kumazaki, Kaoru Fujiwara, Yuichiro Liu, Keihong Nakada-Nakura, Yoshiko Iwata, So Tsukada, Keisuke Komori, Tomotaka Uemura, Sotaro Goto, Yuhei Nakane, Takanori Takemoto, Mizuki Kato, Hideaki E Yamashita, Keitaro Wada, Miki Ito, Koichi Ishitani, Ryuichiro Hattori, Motoyuki Nureki, Osamu Crystal structures of the TRIC trimeric intracellular cation channel orthologues |
title | Crystal structures of the TRIC trimeric intracellular cation channel orthologues |
title_full | Crystal structures of the TRIC trimeric intracellular cation channel orthologues |
title_fullStr | Crystal structures of the TRIC trimeric intracellular cation channel orthologues |
title_full_unstemmed | Crystal structures of the TRIC trimeric intracellular cation channel orthologues |
title_short | Crystal structures of the TRIC trimeric intracellular cation channel orthologues |
title_sort | crystal structures of the tric trimeric intracellular cation channel orthologues |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5143425/ https://www.ncbi.nlm.nih.gov/pubmed/27909292 http://dx.doi.org/10.1038/cr.2016.140 |
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