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Structural Bases for Tetraspanin Functions

  • Michel Seigneuret
  • Hélène Conjeaud
  • Hui-Tang Zhang
  • Xiang-Peng Kong
Chapter
Part of the Proteins and Cell Regulation book series (PROR, volume 9)

Abstract

The tetraspanin transmembrane glycoproteins are considered as “molecular facilitators” which simultaneously interact with, and thereby bring into close proximity specific proteins involved in cellular activation and transduction processes. Elucidation of the 3D structure of tetraspanins is an essential step in understanding of their facilitator function and of the molecular basis of their partner specificity. Although there are currently no experimental atomic resolution structures of a whole tetraspanin molecule, recent information gained from three different approaches has led to a rather comprehensive picture of the structural organization of tetraspanins. These include: (1) crystallographic structures of the main extracellular domain of the ubiquitous tetraspanin CD81; (2) a 6 Å-resolution cryo-EM structure of the tetraspanins uroplakin UPIa and UPIb in the urothelial plaque of mammalian urothelium; (3) molecular modeled-structures of the complete CD81 tetraspanin. On the basis of such structural data, a qualitative view of tetraspanin structure-function relationship is emerging, including a delineation of regions of the molecule involved in specific interactions with partners, as well as an understanding of the structural basis of the multilevel partner specificity of tetraspanins and of the tetraspanin network organization.

Abbreviations

AUM

Asymmetric unit membrane (AUM)

Cryo-EM

Cryo-electron microscopy

EC1

First tetraspanin extracellular region

EC2

Second tetraspanin extracellular region

EM

Electron microscopy

IC

Intracellular

TEM

Tetraspanin-enriched microdomain

TM

Transmembrane

UP

Uroplakin

UPEC

Uropathogenic E. coli

UPIa

Uroplakin Ia

UPIb

Uroplakin Ib

UPII

Uroplakin II

UPIIIa

Uroplakin IIIa

UTI

Urinary tract infection

Notes

Acknowledgments

The work done in the authors’ laboratories was supported by grants from the Centre National de la Recherche Scientifique, the Institut National de la Santé et de la Recherche Médicale, SIDACTION, the Association National pour la Recherche Contre le SIDA (to HC and MS) and NIH grant DK52206 (to HTZ and XPK).

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Copyright information

© Springer Science+Business Media Dordrecht 2013

Authors and Affiliations

  • Michel Seigneuret
    • 1
  • Hélène Conjeaud
    • 1
  • Hui-Tang Zhang
    • 2
  • Xiang-Peng Kong
    • 2
  1. 1.Matière et Systèmes Complexes – CNRS UMR 7057Université Paris-DiderotParis cedex 13France
  2. 2.Department of Biochemistry and Molecular PharmacologyNew York University School of MedicineNew YorkUSA

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