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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.


DOI

doi:10.1111/nyas.13408