4.7 Article

Cryo-EM structure of an open conformation of a gap junction hemichannel in lipid bilayer nanodiscs

期刊

STRUCTURE
卷 29, 期 9, 页码 1040-+

出版社

CELL PRESS
DOI: 10.1016/j.str.2021.05.010

关键词

-

资金

  1. National Institutes of Health (NIH) [R01 HL48908, GM138532, G20 RR31199, S10 RR025067, S10 OD018149, F30 HL129792]
  2. National Institute of General Medical Sciences [P41 GM103311]
  3. University of Virginia

向作者/读者索取更多资源

Connexins play a crucial role in cell-to-cell communication by forming hexameric hemichannels and dodecameric intercellular conduits. The conformational flexibility of extracellular loops is essential for surveillance of hemichannels and intercellular docking.
To mediate cell-to-cell communication via gap junction channels (GJCs), connexins (Cx) traffic as hexameric hemichannels to the plasma membrane, which dock end-to-end between adjacent cell membranes, thereby forming a dodecameric intercellular conduit. Hemichannels also function independently to mediate the passage of contents between the cytoplasm and extracellular space. To generate hemichannels, the mutation N176Y was introduced into the second extracellular loop of Cx26. The electron cryomicroscopy structure of the hexameric hemichannel in lipid bilayer nanodiscs displays an open pore and a 4-helix bundle transmembrane design that is nearly identical to dodecameric GJCs. In contrast to the high resolution of the transmembrane alpha-helices, the extracellular loops are less well resolved. The conformational flexibility of the extracellular loops may be essential to facilitate surveillance of hemichannels in apposed cells to identify compatible Cx isoforms that enable intercellular docking. Our results also provide a structural foundation for previous electrophysiologic and permeation studies of Cx hemichannels.

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。

评论

主要评分

4.7
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据