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Conformational changes and CO2-induced channel gating in connexin26
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Brotherton, Deborah H., Savva, Christos G., Ragan, Timothy J., Dale, Nicholas and Cameron, Alexander D. (2022) Conformational changes and CO2-induced channel gating in connexin26. Structure, 30 (5). 697-706.e4. doi:10.1016/j.str.2022.02.010 ISSN 0969-2126.
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WRAP-conformational-changes-CO2-induced-channel-gating-connexin26-2022.pdf - Published Version - Requires a PDF viewer. Available under License Creative Commons Attribution 4.0. Download (4Mb) | Preview |
Official URL: http://dx.doi.org/10.1016/j.str.2022.02.010
Abstract
Connexins form large-pore channels that function either as dodecameric gap junctions or hexameric hemichannels to allow the regulated movement of small molecules and ions across cell membranes. Opening or closing of the channels is controlled by a variety of stimuli, and dysregulation leads to multiple diseases. An increase in the partial pressure of carbon dioxide (PCO2) has been shown to cause connexin26 (Cx26) gap junctions to close. Here, we use cryoelectron microscopy (cryo-EM) to determine the structure of human Cx26 gap junctions under increasing levels of PCO2. We show a correlation between the level of PCO2 and the size of the aperture of the pore, governed by the N-terminal helices that line the pore. This indicates that CO2 alone is sufficient to cause conformational changes in the protein. Analysis of the conformational states shows that movements at the N terminus are linked to both subunit rotation and flexing of the transmembrane helices.
| Item Type: | Journal Article | |||||||||
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| Subjects: | Q Science > QH Natural history > QH301 Biology Q Science > QP Physiology |
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| Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | |||||||||
| Library of Congress Subject Headings (LCSH): | Connexins, Gap junctions (Cell biology), Electron microscopy -- Technique, Membrane proteins, Proteins -- Structure | |||||||||
| Journal or Publication Title: | Structure | |||||||||
| Publisher: | Cell Press | |||||||||
| ISSN: | 0969-2126 | |||||||||
| Official Date: | 5 May 2022 | |||||||||
| Dates: |
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| Volume: | 30 | |||||||||
| Number: | 5 | |||||||||
| Page Range: | 697-706.e4 | |||||||||
| DOI: | 10.1016/j.str.2022.02.010 | |||||||||
| Status: | Peer Reviewed | |||||||||
| Publication Status: | Published | |||||||||
| Access rights to Published version: | Open Access (Creative Commons) | |||||||||
| Date of first compliant deposit: | 19 May 2022 | |||||||||
| Date of first compliant Open Access: | 24 May 2022 | |||||||||
| RIOXX Funder/Project Grant: |
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