Crystal Structure of a Claudin Provides Insight into the Architecture of Tight Junctions
Crystal Structure of a Claudin Provides Insight into the Architecture of Tight Junctions
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DOI：
10.1126/science.1248571
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发表时间：
2014-04-18
期刊：
影响因子：
56.9
通讯作者：
Fujiyoshi, Yoshinori
中科院分区：
文献类型：
--
作者：
Suzuki, Hiroshi;Nishizawa, Tomohiro;Fujiyoshi, Yoshinori
紧密连接是上皮细胞片层中的细胞-细胞粘附结构，其围绕多细胞生物体中的器官区室并调节离子通过细胞间隙的渗透。紧密连接蛋白是紧密连接的主要组成部分，形成介导细胞粘附的链，并作为细胞旁屏障发挥作用。我们报告的哺乳动物claudin-15的结构在2.4埃的分辨率。该结构揭示了一个特征性的β-折叠折叠，包括两个胞外片段，其通过共有基序锚定到跨膜四螺旋束。我们的分析表明，潜在的细胞外表面上的独特电荷的细胞旁途径，离子稳态的分子基础提供了深入了解整个紧密连接。
Tight junctions are cell-cell adhesion structures in epithelial cell sheets that surround organ compartments in multicellular organisms and regulate the permeation of ions through the intercellular space. Claudins are the major constituents of tight junctions and form strands that mediate cell adhesion and function as paracellular barriers. We report the structure of mammalian claudin-15 at a resolution of 2.4 angstroms. The structure reveals a characteristic beta-sheet fold comprising two extracellular segments, which is anchored to a transmembrane four-helix bundle by a consensus motif. Our analyses suggest potential paracellular pathways with distinctive charges on the extracellular surface, providing insight into the molecular basis of ion homeostasis across tight junctions.