Journal
JOURNAL OF CELL SCIENCE
Volume 119, Issue 23, Pages 4819-4827Publisher
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.03233
Keywords
apical junctional complex; outer hair cell; reticular lamina; organ of Corti; tight-adherens junction; cochlea
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Funding
- NIDCD NIH HHS [R01 DC006262, R01-DC006262] Funding Source: Medline
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Most polarized epithelia constrain solute diffusion between luminal and interstitial compartments using tight junctions and generate mechanical strength using adherens junctions. These intercellular junctions are typically portrayed as incongruent macromolecular complexes with distinct protein components. Herein, we delineate the molecular composition and subdomain architecture of an intercellular junction between sensory and non-sensory cells of the inner ear. In this junction, claudins partition into claudin-14 and claudin-9/6 subdomains that are distinguishable by strand morphology, which contrasts with in vitro data that most claudins co-assemble into heteromeric strands. Surprisingly, canonical adherens junction proteins (p120ctn, alpha- and beta-catenins) colocalize with the claudin-9/6 subdomain and recruit a dense cytoskeletal network. We also find that catenins colocalize with claudin-9 and claudin-6, but not claudin-14, in a heterologous system. Together, our data demonstrate that canonical tight junction and adherens junction proteins can be recruited to a single junction in which claudins partition into subdomains and form a novel hybrid tight junction with adherens junction organization.
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