Structural highlights
Disease
[MALD2_HUMAN] Autosomal recessive non-syndromic sensorineural deafness type DFNB. The disease is caused by mutations affecting the gene represented in this entry.
Function
[MALD2_HUMAN] Plays a role in the formation of the epithelial barriers. The separation of the endolymphatic and perilymphatic spaces of the organ of Corti from one another by epithelial barriers is required for normal hearing.[1]
Publication Abstract from PubMed
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.
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. 2017 Jun 29. doi: 10.1111/nyas.13408. PMID:28661558[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Riazuddin S, Ahmed ZM, Fanning AS, Lagziel A, Kitajiri S, Ramzan K, Khan SN, Chattaraj P, Friedman PL, Anderson JM, Belyantseva IA, Forge A, Riazuddin S, Friedman TB. Tricellulin is a tight-junction protein necessary for hearing. Am J Hum Genet. 2006 Dec;79(6):1040-51. Epub 2006 Oct 31. PMID:17186462 doi:http://dx.doi.org/10.1086/510022
- ↑ Schuetz A, Radusheva V, Krug SM, Heinemann U. Crystal structure of the tricellulin C-terminal coiled-coil domain reveals a unique mode of dimerization. Ann N Y Acad Sci. 2017 Jun 29. doi: 10.1111/nyas.13408. PMID:28661558 doi:http://dx.doi.org/10.1111/nyas.13408
