Depolarization induces a conformational change in the binding site region of the M2 muscarinic receptor.

ABSTRACT: G protein-coupled receptors play a central role in signal transduction and were only known to be activated by agonists. Recently it has been shown that membrane potential also affects the activity of G protein-coupled receptors. For the M(2) muscarinic receptor, it was further shown that depolarization induces charge movement. A tight correlation was found between the voltage-dependence of the charge movement and the voltage-dependence of the agonist binding. Here we examine whether depolarization-induced charge movement causes a conformational change in the M(2) receptor that may be responsible for the voltage-dependence of agonist binding. Using site-directed fluorescence labeling we show a voltage-dependent fluorescence signal, reflecting a conformational change, which correlates with t

SUBMITTER: Dekel N 

PROVIDER: S-EPMC3252955 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature