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Forskolin Modulates Acetylcholine Receptor Gating by Interacting with the Small Extracellular Loop Between the M2 and M3 Transmembrane Domains
Journal article   Open access   Peer reviewed

Forskolin Modulates Acetylcholine Receptor Gating by Interacting with the Small Extracellular Loop Between the M2 and M3 Transmembrane Domains

Zhaoming Chen and Michael White
Cellular and molecular neurobiology, v 20(5), pp 569-577
Oct 2000
PMID: 10930133
url
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11537508View
Published, Version of Record (VoR)Open Access (License Unspecified) Open

Abstract

Life Sciences chimeric subunits forskolin Neurosciences transduction nicotinic acetylcholine receptors Animal Anatomy / Morphology / Histology allosteric modulator
1. Forskolin acts as an allosteric modulator of muscle-type nicotinic acetylcholine receptors. Receptors from mouse muscle and Torpedo electroplax demonstrate differential sensitivity to inhibition by forskolin. Previous work from this laboratory suggested that the γ subunit is responsible for this differential sensitivity.2. We have used a series of mouse/Torpedo species-chimeric γ subunits to further define the site of forskolin interaction with the γ subunit. Analysis of the patterns of forskolin inhibition of receptors containing mouse/Torpedo chimeric γ subunits along with the mouse α, β, and δ subunits suggests that forskolin interacts with the small extracellular domain that links the M2 and M3 transmembrane domains (the M2–M3 linker).3. We suggest that the M2–M3 linker domain plays an important role in the transduction of ligand binding to the conformational changes that result in channel opening.

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Web of Science research areas
Cell Biology
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