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Crystal structure of the tricellulin C-terminal coiled-coil domain reveals a unique mode of dimerization.

Schuetz A, Radusheva V, Krug SM, Heinemann U
Ann N Y Acad Sci 1405 147-159 (2017)
Related entries: 5n7h, 5n7i

Cited: 4 times
EuropePMC logo PMID: 28661558

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.

Reviews - 5n7k mentioned but not cited (1)

  1. Structural Features of Tight-Junction Proteins. Heinemann U, Schuetz A. Int J Mol Sci 20 E6020 (2019)


Articles citing this publication (3)

  1. Apoptotic Fragmentation of Tricellulin. Janke S, Mittag S, Reiche J, Huber O. Int J Mol Sci 20 E4882 (2019)
  2. Chimeric Claudins: A New Tool to Study Tight Junction Structure and Function. Taylor A, Warner M, Mendoza C, Memmott C, LeCheminant T, Bailey S, Christensen C, Keller J, Suli A, Mizrachi D. Int J Mol Sci 22 4947 (2021)
  3. Association of tricellulin expression with poor colorectal cancer prognosis and metastasis. Zhang JX, Qin MB, Ye Z, Peng P, Li SM, Song Q, Lin L, Liu SQ, Xie LH, Zhu Y, Huang JA. Oncol Rep 44 2174-2184 (2020)


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