Differential pathways of claudin oligomerization and integration into tight junctions

• Type of Material: Article
• Authors: Michael H Koval, Emory University
• Language: English
• Date: 2013-07-01
• Publisher: Landes Bioscience
• Publication Version: Final Published Version
• Copyright Statement: © 2013 Landes Bioscience
• License: Creative Commons Attribution-Noncommercial 3.0 Unported
• Final Published Version (URL): https://www.landesbioscience.com/journals/tissuebarriers/article/24518/
• Title of Journal or Parent Work: Tissue Barriers
• ISSN: 2168-8362
• Volume: 1
• Issue: 3
• Start Page: e24518
• End Page: e24518
• Grant/Funding Information: This work was supported by National Institutes of Health grants HL-083120, AA-013757 and by the Emory University Research Committee.
• Keywords: tight junction; quality control; claudin; assembly; intracellular transport
• Research Categories: Biology, Cell; Health Sciences, General

Abstract

Tight junctions are the critical intercellular structure required to establish an epithelial barrier. Among the several classes of proteins required to form tight junctions are the tetraspan transmembrane proteins known as claudins that directly determine paracellular permeability. Considerable progress has been made in understanding how incorporation of different claudins into tight junctions increase or decrease paracellular permeability and ion selectivity. However, it has proven difficult to identify discrete steps in claudin assembly and whether claudins exist in distinct oligomerization states prior to tight junction assembly. Studies of homomeric and heteromeric claudin-claudin interactions using complementary techniques suggest a diversity of pathways used by different claudins to oligomerize and integrate into tight junctions.