Intrapore lipids hydrophobically gate pannexin-1 channels-Reference-Cited by-同舟云学术

Intrapore lipids hydrophobically gate pannexin-1 channels

Published:2022-02-08 Issue:720 Volume:15 Page:
ISSN:1945-0877
Container-title:Science Signaling
language:en
Short-container-title:Sci. Signal.

Author:

Anderson Connor L.¹^ORCID,Thompson Roger J.¹

Affiliation:

1. Department of Cell Biology and Anatomy and Hotchkiss Brain Institute, Cumming School of Medicine, University of Calgary, 3330 Hospital Dr. NW, Calgary, Alberta, T2N 1N4, Canada.

Abstract

Large-pore channels such as pannexin-1 (PANX1) typically lack pore-lining constriction points, leaving only speculations on how these channels functionally “close.” In this issue of Science Signaling , Kuzuya et al . found that rearrangements in the PANX1 amino-terminal helix mediate channel gating by a surprising mechanism in which lipids block the ion conduction pathway, creating a hydrophobic gate.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference8 articles.

1. On the molecular nature of large-pore channels

2. Structures of human pannexin-1 in nanodiscs reveal gating mediated by dynamic movement of the N terminus and phospholipids

3. Structures of human pannexin 1 reveal ion pathways and mechanism of gating

4. Cryo-EM structures of the ATP release channel pannexin 1

5. Cryo-EM structures of undocked innexin-6 hemichannels in phospholipids

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