Glycosylation of β1 subunit plays a pivotal role in the toxin sensitivity and activation of BK channels.

ABSTRACT:

Background

The accessory β1 subunits, regulating the pharmacological and biophysical properties of BK channels, always undergo post-translational modifications, especially glycosylation. To date, it remains elusive whether the glycosylation contributes to the regulation of BK channels by β1 subunits.

Methods

Herein, we combined the electrophysiological approach with molecular mutations and biochemical manipulation to investigate the function roles of N-glycosylation in β1 subunits.

Results

The results show that deglycosylation of β1 subunits through double-site mutations (β1 N80A/N142A or β1 N80Q/N142Q) could significantly increase the inhibitory potency of iberiotoxin, a specific BK channel blocker. The deglycosylated channels also have a different sensitivity to mar

SUBMITTER: Wang X 

PROVIDER: S-EPMC8183112 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature