Morphologic determinant of tight junctions revealed by claudin-3 structures

Shun Nakamura, Katsumasa Irie, Hiroo Tanaka, Kouki Nishikawa, Hiroshi Suzuki, Yasunori Saitoh, Atsushi Tamura, Sachiko Tsukita and Yoshinori Fujiyoshi ()
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Shun Nakamura: Nagoya University
Katsumasa Irie: Nagoya University
Hiroo Tanaka: Osaka University
Kouki Nishikawa: Nagoya University
Hiroshi Suzuki: Nagoya University
Yasunori Saitoh: Nagoya University
Atsushi Tamura: Osaka University
Sachiko Tsukita: Osaka University
Yoshinori Fujiyoshi: Nagoya University

Nature Communications, 2019, vol. 10, issue 1, 1-10

Abstract: Abstract Tight junction is a cell adhesion apparatus functioning as barrier and/or channel in the paracellular spaces of epithelia. Claudin is the major component of tight junction and polymerizes to form tight junction strands with various morphologies that may correlate with their functions. Here we present the crystal structure of mammalian claudin-3 at 3.6 Å resolution. The third transmembrane helix of claudin-3 is clearly bent compared with that of other subtypes. Structural analysis of additional two mutants with a single mutation representing other subtypes in the third helix indicates that this helix takes a bent or straight structure depending on the residue. The presence or absence of the helix bending changes the positions of residues related to claudin-claudin interactions and affects the morphology and adhesiveness of the tight junction strands. These results evoke a model for tight junction strand formation with different morphologies – straight or curvy strands – observed in native epithelia.

Date: 2019
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DOI: 10.1038/s41467-019-08760-7

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