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Semin Cell Dev Biol. 2015 Jun;42:3-12. doi: 10.1016/j.semcdb.2015.04.010. Epub 2015 May 7.

Assembly and function of claudins: Structure-function relationships based on homology models and crystal structures.

Author information

1
Leibnitz-Institut fuer molekulare Pharmakologie (FMP), 13125 Berlin, Germany. Electronic address: GKrause@fmp-berlin.de.
2
Leibnitz-Institut fuer molekulare Pharmakologie (FMP), 13125 Berlin, Germany.
3
Institute of Clinical Physiology, Charité - Universitätsmedizin Berlin, 12203 Berlin, Germany.

Abstract

The tetra-span transmembrane proteins of the claudin family are critical components of formation and function of tight junctions (TJ). Homo- and heterophilic side-by-side (cis) and intercellular head-to-head (trans) interactions of 27 claudin-subtypes regulate tissue-specifically the paracellular permeability and/or tightness between epithelial or endothelial cells. This review highlights the functional impact that has been identified for particular claudin residues by relating them to structural features and architectural characteristics in the light of structural advances, which have been contributed by homology models, cryo-electron microscopy and crystal structures. The differing contributions to the TJ functionalities by claudins are dissected for the transmembrane region, the first and the second extracellular loop of claudins separately. Their particular impact to oligomerisation and TJ strand- and pore-formation is surveyed. Detailed knowledge about structure-function relationships about claudins helps to reveal the molecular mechanisms of TJ assembly and regulation of paracellular permeability, which is yet not fully understood.

KEYWORDS:

Clostridium perfringens enterotoxin; Paracellular permeability; Pore formation; Strand assembly, -disassembly; Tight junction proteins

PMID:
25957516
DOI:
10.1016/j.semcdb.2015.04.010
[Indexed for MEDLINE]

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