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...

Celý popis

Uložené v:

Podrobná bibliografia
Vydané v:	Nature communications Ročník 11; číslo 1; s. 1606 - 11
Hlavní autori:	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
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	London Nature Publishing Group UK 30.03.2020 Nature Publishing Group Nature Portfolio
Predmet:	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
On-line prístup:	Získať plný text
Tagy:	Pridať tag Žiadne tagy, Buďte prvý, kto otaguje tento záznam!

Popis
Shrnutí:	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.
Bibliografia:	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