Distinct subdomain organization and molecular composition of a tight junction with adherens junction features
| Autor: | Fábio Daumas Nunes, Ricardo Bentes Azevedo, Alexander Gow, Bechara Kachar, Caroline Davies, Lanier N. Lopez, Harrison W. Lin |
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| Rok vydání: | 2006 |
| Předmět: |
Delta Catenin
endocrine system diseases Guinea Pigs Septate junctions Biology urologic and male genital diseases digestive system Cell junction Basement Membrane Tight Junctions Adherens junction Mice Chlorocebus aethiops Animals Protein Structure Quaternary Claudin Cytoskeleton beta Catenin Hair Cells Auditory Inner Tight junction Vestibular Nucleus Lateral Membrane Proteins Catenins Adherens Junctions Cell Biology Phosphoproteins Actins digestive system diseases Protein Structure Tertiary Rats Cell biology Hair Cells Auditory Outer Intercellular Junctions Ear Inner Catenin COS Cells Claudins Cell Adhesion Molecules tissues Adherens junction organization |
| Zdroj: | Journal of Cell Science. 119:4819-4827 |
| ISSN: | 1477-9137 0021-9533 |
| DOI: | 10.1242/jcs.03233 |
| Popis: | 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, α- and β-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. |
| Databáze: | OpenAIRE |
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