The fifth subunit of the (α4β2)₂ β2 nicotinic ACh receptor modulates maximal ACh responses.

ABSTRACT:

Background and purpose

The fifth subunit in the (α4β2)₂ α4 nicotinic ACh receptor (nAChR) plays a determining role in the pharmacology of this nAChR type. Here, we have examined the role of the fifth subunit in the ACh responses of the (α4β2)₂ β2 nAChR type.

Experimental approach

The role of the fifth subunit in receptor function was explored using two-electrode voltage clamp electrophysiology, along with subunit-targeted mutagenesis and the substituted cysteine scanning method applied to fully linked (α4β2)₂ β2 receptors.

Key results

Covalent modification of the cysteine-substituted fifth subunit with a thiol-reactive agent (MTS) caused irreversible inhibition of receptor function. ACh reduced the rate of the reaction to MTS, but the

SUBMITTER: New K 

PROVIDER: S-EPMC5978951 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature