Crystal structure of the tricellulin C-terminal coiled-coil domain reveals a unique mode of dimerization.
Authors
- A. Schuetz
- V. Radusheva
- S.M. Krug
- U. Heinemann
Journal
- Annals of the New York Academy of Sciences
Citation
- Ann N Y Acad Sci 1405 (1): 147-159
Abstract
Tricellulin is a tight junction protein localized to tricellular contacts in many epithelial tissues, where it is required for full barrier control. Here, we present crystal structures of the tricellulin C-terminal coiled-coil domain, revealing a potential dimeric arrangement. By combining structural, biochemical, functional, and mutation analyses, we gain insight into the mode of tricellulin oligomerization and suggest a model where dimerization of its cytoplasmic C-terminus may play an auxiliary role in stabilizing homophilic and potentially also heterophilic cis-interactions within tight junctions.