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© Marie Prévost, Institut Pasteur
Image of a portion of a Xenopus oocyte expressing a channel receptor.
Publication : Proceedings of the National Academy of Sciences of the United States of America

Structural titration of receptor ion channel GLIC gating by HS-AFM

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Proceedings of the National Academy of Sciences of the United States of America - 04 Sep 2018

Ruan Y, Kao K, Lefebvre S, Marchesi A, Corringer PJ, Hite RK, Scheuring S

Link to Pubmed [PMID] – 30181288

Proc. Natl. Acad. Sci. U.S.A. 2018 10;115(41):10333-10338

ligand-gated ion channel (GLIC), a proton-gated, cation-selective channel, is a prokaryotic homolog of the pentameric Cys-loop receptor ligand-gated ion channel family. Despite large changes in ion conductance, small conformational changes were detected in X-ray structures of detergent-solubilized GLIC at pH 4 (active/desensitized state) and pH 7 (closed state). Here, we used high-speed atomic force microscopy (HS-AFM) combined with a buffer exchange system to perform structural titration experiments to visualize GLIC gating at the single-molecule level under native conditions. Reference-free 2D classification revealed channels in multiple conformational states during pH gating. We find changes of protein-protein interactions so far elusive and conformational dynamics much larger than previously assumed. Asymmetric pentamers populate early stages of activation, which provides evidence for an intermediate preactivated state.

https://www.ncbi.nlm.nih.gov/pubmed/30181288