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Structural insights into tetraspanin CD9 function
Tetraspanins play critical roles in various physiological processes, ranging from cell adhesion to virus infection. The members of the tetraspanin family have four membrane-spanning domains and short and large extracellular loops, and associate with a broad range of other functional proteins to exer...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7105497/ https://www.ncbi.nlm.nih.gov/pubmed/32231207 http://dx.doi.org/10.1038/s41467-020-15459-7 |
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author | Umeda, Rie Satouh, Yuhkoh Takemoto, Mizuki Nakada-Nakura, Yoshiko Liu, Kehong Yokoyama, Takeshi Shirouzu, Mikako Iwata, So Nomura, Norimichi Sato, Ken Ikawa, Masahito Nishizawa, Tomohiro Nureki, Osamu |
author_facet | Umeda, Rie Satouh, Yuhkoh Takemoto, Mizuki Nakada-Nakura, Yoshiko Liu, Kehong Yokoyama, Takeshi Shirouzu, Mikako Iwata, So Nomura, Norimichi Sato, Ken Ikawa, Masahito Nishizawa, Tomohiro Nureki, Osamu |
author_sort | Umeda, Rie |
collection | PubMed |
description | Tetraspanins play critical roles in various physiological processes, ranging from cell adhesion to virus infection. The members of the tetraspanin family have four membrane-spanning domains and short and large extracellular loops, and associate with a broad range of other functional proteins to exert cellular functions. Here we report the crystal structure of CD9 and the cryo-electron microscopic structure of CD9 in complex with its single membrane-spanning partner protein, EWI-2. The reversed cone-like molecular shape of CD9 generates membrane curvature in the crystalline lipid layers, which explains the CD9 localization in regions with high membrane curvature and its implications in membrane remodeling. The molecular interaction between CD9 and EWI-2 is mainly mediated through the small residues in the transmembrane region and protein/lipid interactions, whereas the fertilization assay revealed the critical involvement of the LEL region in the sperm-egg fusion, indicating the different dependency of each binding domain for other partner proteins. |
format | Online Article Text |
id | pubmed-7105497 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-71054972020-04-01 Structural insights into tetraspanin CD9 function Umeda, Rie Satouh, Yuhkoh Takemoto, Mizuki Nakada-Nakura, Yoshiko Liu, Kehong Yokoyama, Takeshi Shirouzu, Mikako Iwata, So Nomura, Norimichi Sato, Ken Ikawa, Masahito Nishizawa, Tomohiro Nureki, Osamu Nat Commun Article Tetraspanins play critical roles in various physiological processes, ranging from cell adhesion to virus infection. The members of the tetraspanin family have four membrane-spanning domains and short and large extracellular loops, and associate with a broad range of other functional proteins to exert cellular functions. Here we report the crystal structure of CD9 and the cryo-electron microscopic structure of CD9 in complex with its single membrane-spanning partner protein, EWI-2. The reversed cone-like molecular shape of CD9 generates membrane curvature in the crystalline lipid layers, which explains the CD9 localization in regions with high membrane curvature and its implications in membrane remodeling. The molecular interaction between CD9 and EWI-2 is mainly mediated through the small residues in the transmembrane region and protein/lipid interactions, whereas the fertilization assay revealed the critical involvement of the LEL region in the sperm-egg fusion, indicating the different dependency of each binding domain for other partner proteins. Nature Publishing Group UK 2020-03-30 /pmc/articles/PMC7105497/ /pubmed/32231207 http://dx.doi.org/10.1038/s41467-020-15459-7 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Umeda, Rie Satouh, Yuhkoh Takemoto, Mizuki Nakada-Nakura, Yoshiko Liu, Kehong Yokoyama, Takeshi Shirouzu, Mikako Iwata, So Nomura, Norimichi Sato, Ken Ikawa, Masahito Nishizawa, Tomohiro Nureki, Osamu Structural insights into tetraspanin CD9 function |
title | Structural insights into tetraspanin CD9 function |
title_full | Structural insights into tetraspanin CD9 function |
title_fullStr | Structural insights into tetraspanin CD9 function |
title_full_unstemmed | Structural insights into tetraspanin CD9 function |
title_short | Structural insights into tetraspanin CD9 function |
title_sort | structural insights into tetraspanin cd9 function |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7105497/ https://www.ncbi.nlm.nih.gov/pubmed/32231207 http://dx.doi.org/10.1038/s41467-020-15459-7 |
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