Angulin-1 seals tricellular contacts independently of tricellulin and claudins |
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Authors: | Taichi Sugawara Kyoko Furuse Tetsuhisa Otani Tomohiko Wakayama Mikio Furuse |
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Institution: | 1. Division of Cell Structure, National Institute for Physiological Sciences, National Institute of Natural Sciences, Okazaki, Aichi, Japan ; 2. Department of Physiological Sciences, The Graduate University for Advanced Studies, SOKENDAI, Okazaki, Aichi, Japan ; 3. Department of Histology, Graduate School of Medical Sciences, Kumamoto University, Kumamoto, Japan |
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Abstract: | Tricellular tight junctions (tTJs) are specialized tight junctions (TJs) that seal the intercellular space at tricellular contacts (TCs), where the vertices of three epithelial cells meet. Tricellulin and angulin family membrane proteins are known constituents of tTJs, but the molecular mechanism of tTJ formation remains elusive. Here, we investigated the roles of angulin-1 and tricellulin in tTJ formation in MDCK II cells by genome editing. Angulin-1–deficient cells lost the plasma membrane contact at TCs with impaired epithelial barrier function. The C terminus of angulin-1 bound to the TJ scaffold protein ZO-1, and disruption of their interaction influenced the localization of claudins at TCs, but not the tricellular sealing. Strikingly, the plasma membrane contact at TCs was formed in tricellulin- or claudin-deficient cells. These findings demonstrate that angulin-1 is responsible for the plasma membrane seal at TCs independently of tricellulin and claudins. |
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