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Author Westphal, Julie K. ♦ Dörfel, Max J. ♦ Krug, Susanne M. ♦ Cording, Jimmi D. ♦ Piontek, Jörg ♦ Blasig, Ingolf E. ♦ Tauber, Rudolf ♦ Fromm, Michael ♦ Huber, Otmar
Source SpringerLink
Content type Text
Publisher SP Birkhäuser Verlag Basel
File Format PDF
Copyright Year ©2010
Language English
Subject Domain (in DDC) Natural sciences & mathematics ♦ Life sciences; biology
Subject Keyword Tricellulin ♦ Occludin ♦ Tight junction ♦ Tricellular contacts ♦ Barrier ♦ Biochemistry ♦ Life Sciences ♦ Biomedicine general ♦ Cell Biology
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.
ISSN 1420682X
Age Range 18 to 22 years ♦ above 22 year
Educational Use Research
Education Level UG and PG
Learning Resource Type Article
Publisher Date 2010-03-07
Publisher Place Basel
e-ISSN 14209071
Journal Cellular and Molecular Life Sciences
Volume Number 67
Issue Number 12
Page Count 12
Starting Page 2057
Ending Page 2068


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Source: SpringerLink