A Novel Voltage Sensor in the Orthosteric Binding Site of the M2 Muscarinic Receptor

Biophys J. 2016 Oct 4;111(7):1396-1408. doi: 10.1016/j.bpj.2016.08.035.

Abstract

G protein-coupled receptors (GPCRs) mediate many signal transduction processes in the body. The discovery that these receptors are voltage-sensitive has changed our understanding of their behavior. The M2 muscarinic acetylcholine receptor (M2R) was found to exhibit depolarization-induced charge movement-associated currents, implying that this prototypical GPCR possesses a voltage sensor. However, the typical domain that serves as a voltage sensor in voltage-gated channels is not present in GPCRs, making the search for the voltage sensor in the latter challenging. Here, we examine the M2R and describe a voltage sensor that is comprised of tyrosine residues. This voltage sensor is crucial for the voltage dependence of agonist binding to the receptor. The tyrosine-based voltage sensor discovered here constitutes a noncanonical by which membrane proteins may sense voltage.

MeSH terms

  • Animals
  • Binding Sites
  • Calcium / chemistry
  • Calcium / metabolism
  • Chlorine / chemistry
  • Chlorine / metabolism
  • Electricity
  • Ions / chemistry
  • Ions / metabolism
  • Membrane Potentials / drug effects
  • Membrane Potentials / physiology*
  • Models, Molecular
  • Muscarinic Agonists / chemistry
  • Muscarinic Agonists / pharmacology
  • Mutation
  • Oocytes / chemistry
  • Oocytes / drug effects
  • Oocytes / physiology
  • Patch-Clamp Techniques
  • Pilocarpine / chemistry
  • Pilocarpine / pharmacology
  • Protein Conformation
  • Protein Domains
  • Receptor, Muscarinic M2 / agonists
  • Receptor, Muscarinic M2 / chemistry
  • Receptor, Muscarinic M2 / genetics
  • Receptor, Muscarinic M2 / metabolism*
  • Tyrosine / chemistry
  • Tyrosine / metabolism
  • Xenopus

Substances

  • Ions
  • Muscarinic Agonists
  • Receptor, Muscarinic M2
  • Pilocarpine
  • Tyrosine
  • Chlorine
  • Calcium