Distinct domains of LINGO1 control surface expression and biophysical properties of large conductance Ca²⁺- and voltage-activated potassium (BK) channels.

ABSTRACT: Large conductance Ca²⁺ and voltage-activated K⁺ (BK) channels are ubiquitous ion channels that regulate a wide array of physiological process. Their functional diversity can be modulated by accessory proteins including a family of leucine-rich repeat and immunoglobulin-like domain-containing protein (LINGO) subunits that may control both the biophysical properties and surface trafficking of BK channels. By exploiting differences in the regulation of BK channels by LINGO1 and LINGO2 subunits we have taken a chimeric approach to dissect the role of distinct domains of these single transmembrane pass proteins. We demonstrate that the large extracellular domain of LINGO1, but not the transmembrane or intracellular C-terminal tail domain (ITD), is required to inhibit plasm

SUBMITTER: Al Kawadri Y 

PROVIDER: S-EPMC12423400 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature