Cholesterol sensitivity of KIR2.1 depends on functional inter-links between the N and C termini.

ABSTRACT: In recent years, cholesterol has been emerging as a major regulator of ion channel function. We have previously shown that cholesterol suppresses Kir2 channels, a subfamily of constitutively active strongly rectifying K (+) channels. Furthermore, our earlier studies have shown that cholesterol sensitivity of Kir2 channels depends on a group of residues that form a belt-like structure around the cytosolic pore of the channel in proximity to the transmembrane domain. In this study, we focus on the contributions of different structural domains of Kir2 channels in the regulation of their cholesterol sensitivity. Focusing on the mildest mutation in the sensitivity belt, L222I, we show that the sensitivity of the channel to cholesterol can be restored by crosstalk between three distinct cytosoli

SUBMITTER: Rosenhouse-Dantsker A 

PROVIDER: S-EPMC3989358 | biostudies-literature | 2013 Jul-Aug

REPOSITORIES: biostudies-literature