Journal
BIOCHEMICAL JOURNAL
Volume 464, Issue -, Pages 49-60Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20140431
Keywords
claudin; homology modelling; membrane protein; mutagenesis; tight junction
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Funding
- Deutsche Forschungsgemeinschaft [PI 837/2-1, KR 1273/3-2 (FOR 721/2)]
- Forschungsverbund Berlin e.V
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The mechanism of TJ (tight junction) assembly and the structure of TJ strand-forming Cldns (claudins) are unclear. To identify determinants of assembly of blood-brain barrier-related Cldn3 and Cldn5, chimaeric mutants were analysed by cellular reconstitution of TJ strands and live-cell imaging. On the basis of the rescue of mutants deficient for strand formation, we identified Cldn5 residues (Cys(128), Ala(132), Ile(142), Ala(163), Ile(166) and Len(174)) involved in Cldn folding and assembly. Experimental results were combined with structural bioinformatics approaches. Initially the experimentally validated previous model of the ECL2 (extracellular loop 2) of Cldn5 was extended to the flanking transmembrane segments (TM3/TM4). A coiled-coil interface probably caused by alternating small and large residues is supported by concomitant knob-into-hole interactions including
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