期刊
MOLECULAR BIOLOGY OF THE CELL
卷 26, 期 24, 页码 4333-4346出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E15-06-0422
关键词
-
类别
资金
- National Institutes of Health [RO1DK084059, P30 DK079333, R21DK082990]
- American Heart Association [0930050N]
The molecular nature of tight junction architecture and permeability is a long-standing mystery. Here, by comprehensive biochemical, biophysical, genetic, and electron microscopic analyses of claudin-16 and -19 interactions-two claudins that play key polygenic roles in fatal human renal disease, FHHNC-we found that 1) claudin-16 and -19 form a stable dimer through cis association of transmembrane domains 3 and 4; 2) mutations disrupting the claudin-16 and -19 cis interaction increase tight junction ultrastructural complexity but reduce tight junction permeability; and 3) no claudin hemichannel or heterotypic channel made of claudin-16 and -19 trans interaction can exist. These principles can be used to artificially alter tight junction permeabilities in various epithelia by manipulating selective claudin interactions. Our study also emphasizes the use of a novel recording approach based on scanning ion conductance microscopy to resolve tight junction permeabilities with submicrometer precision.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据