Tricellulin forms homomeric and heteromeric tight junctional complexes |
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Authors: | Julie K Westphal Max J Dörfel Susanne M Krug Jimmi D Cording Jörg Piontek Ingolf E Blasig Rudolf Tauber Michael Fromm Otmar Huber |
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Institution: | 1. Institute of Biochemistry II, Jena University Hospital, Nonnenplan 2, 07743, Jena, Germany 2. Institute of Laboratory Medicine and Pathobiochemistry, Charité-Universit?tsmedizin Berlin, Berlin, Germany 3. Institute of Clinical Physiology, Charité-Universit?tsmedizin Berlin, Berlin, Germany 4. Leibniz-Institute of Molecular Pharmacology (FMP), Berlin-Buch, Berlin, Germany
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Abstract: | Sealing of the paracellular cleft by tight junctions is of central importance for epithelia and endothelia to function as
efficient barriers between the extracellular space and the inner milieu. Occludin and claudins represent the major tight junction
components involved in establishing this barrier function. A special situation emerges at sites where three cells join together.
Tricellulin, a recently identified tetraspan protein concentrated at tricellular contacts, was reported to organize tricellular
as well as bicellular tight junctions. Here we show that in MDCK cells, the tricellulin C-terminus is important for the basolateral
translocation of tricellulin, whereas the N-terminal domain appears to be involved in directing tricellulin to tricellular
contacts. In this respect, identification of homomeric tricellulin-tricellulin and of heteromeric tricellulin-occludin complexes
extends a previously published model and suggests that tricellulin and occludin are transported together to the edges of elongating
bicellular junctions and get separated when tricellular contacts are formed. |
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