Occludin is an integral membrane protein concentrated at tight junctions, where neighbouring epithelial or endothelial cells regulate passage between them. It has four membrane-spanning segments and a long cytoplasmic tail. Occludin is a junction component rather than a synonym for the entire sealing structure.
In 1993, Mikio Furuse and colleagues raised monoclonal antibodies against a junction-enriched fraction from chick liver. Immunoelectron microscopy placed the recognized protein directly at membrane-contact points of tight junctions; sequence analysis suggested four membrane crossings. These combined biochemical and spatial observations identified occludin.[ref]
Occludin: a novel integral membrane protein localizing at tight junctions by Mikio Furuse and others. Abstract, pp. 1777–1788: fractionation, antibody localization and cDNA sequence
Later, expression of claudin-1 or claudin-2 in fibroblasts reconstituted extensive junction strands and recruited occludin. This separates the capacity to build a strand from the presence of one particular strand-associated protein.[ref]
A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts by Mikio Furuse and others. 1998, abstract: claudin reconstitution and occludin recruitment
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