Distinct subdomain organization and molecular composition of a tight junction with adherens junction features
Distinct subdomain organization and molecular composition of a tight junction with adherens junction features
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DOI：
10.1242/jcs.03233
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发表时间：
2006-12-01
影响因子：
4
通讯作者：
Kachar, Bechara
中科院分区：
文献类型：
--
作者：
Nunes, Fabio D.;Lopez, Lanier N.;Kachar, Bechara
大多数极化上皮细胞使用紧密连接限制管腔和间质隔室之间的溶质扩散，并使用粘附连接产生机械强度。这些细胞间连接通常被描绘为具有不同蛋白质组分的不一致的大分子复合物。在此，我们描绘了内耳感觉和非感觉细胞之间的细胞间连接的分子组成和亚结构域架构。在该连接处，密蛋白分区成密蛋白-14和密蛋白-9/6亚结构域，其通过链形态可区分，这与大多数密蛋白共组装成异聚链的体外数据形成对比。令人惊讶的是，典型的粘附连接蛋白（p120 ctn，α-和β-连环蛋白）与claudin-9/6亚结构域共定位，并招募密集的细胞骨架网络。我们还发现，连环蛋白共定位与claudin-9和claudin-6，但不claudin-14，在异源系统。总之，我们的数据表明，典型的紧密连接和粘附连接蛋白可以被招募到一个单一的连接，其中claudins分区成亚结构域，并形成一个新的混合紧密连接与粘附连接组织。
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.