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Letter
Nature 444, 106-109 (2 November 2006) | doi:10.1038/nature05259; Received 26 July 2006; Accepted 18 September 2006; Published online 25 October 2006
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Movement of 'gating charge' is coupled to ligand binding in a G-protein-coupled receptor
Yair Ben-Chaim1,5, Baron Chanda2, Nathan Dascal3, Francisco Bezanilla4, Itzchak Parnas1 & Hanna Parnas1
- Department of Neurobiology, The Hebrew University, Jerusalem, 91904, Israel
- Department of Physiology, University of Wisconsin, Madison, Wisconsin 53706, USA
- Department of Physiology and Pharmacology, Tel Aviv University, Tel-Aviv, 69978, Israel
- Institute for Molecular Pediatric Sciences, University of Chicago, Chicago, Illinois 60637, USA
- Present address: Neuroscience Department, The John Hopkins University Medical School, Baltimore, MD21205, USA
Correspondence to: Hanna Parnas1 Correspondence and requests for materials should be addressed to H.P. (Email: hannap@huji.ac.il).
Abstract
Activation by agonist binding of G-protein-coupled receptors (GPCRs) controls most signal transduction processes1. Although these receptors span the cell membrane, they are not considered to be voltage sensitive. Recently it was shown that both the activity of GPCRs2, 3, 4, 5 and their affinity towards agonists6 are regulated by membrane potential. However, it remains unclear whether GPCRs intrinsically respond to changes in membrane potential. Here we show that two prototypical GPCRs, the m2 and m1 muscarinic receptors (m2R and m1R), display charge-movement-associated currents analogous to 'gating currents' of voltage-gated channels. The gating charge–voltage relationship of m2R correlates well with the voltage dependence of the affinity of the receptor for acetylcholine. The loop that couples m2R and m1R to their G protein has a crucial function in coupling voltage sensing to agonist-binding affinity. Our data strongly indicate that GPCRs serve as sensors for both transmembrane potential and external chemical signals.
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