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...

Full description

Saved in:
Bibliographic Details
Published in:Nature communications Vol. 11; no. 1; pp. 1606 - 11
Main Authors: 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
Format: Journal Article
Language:English
Published: London Nature Publishing Group UK 30.03.2020
Nature Publishing Group
Nature Portfolio
Subjects:
101/28
631/535/1258
631/535/1266
631/80
Adhesion
Animals
Antigens, CD - chemistry
CD9 antigen
Cell adhesion
Cell adhesion & migration
Cell Adhesion - physiology
Cell fusion
Cellular structure
Cryoelectron Microscopy
Crystal structure
Crystallography, X-Ray
Curvature
Female
Fertilization
Fertilization - physiology
Functionals
Humanities and Social Sciences
Humans
Lipids
Localization
Male
Membrane proteins
Membrane Proteins - chemistry
Membrane Proteins - metabolism
Membranes
Mice
Mice, Knockout
Models, Molecular
Molecular interactions
multidisciplinary
Physiology
Protein Conformation
Proteins
Science
Science (multidisciplinary)
Tetraspanin 29 - chemistry
Tetraspanin 29 - genetics
Tetraspanin 29 - physiology
Viruses
ISSN:2041-1723, 2041-1723
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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. Tetraspanins play critical roles in various physiological processes, ranging from cell adhesion to virus infection. Here authors 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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 14
content type line 23
ISSN:2041-1723
2041-1723
DOI:10.1038/s41467-020-15459-7