Interaction with stomatin directs human proton channels into cholesterol-dependent membrane domains.

ABSTRACT: Many membrane proteins are modulated by cholesterol. Here we report profound effects of cholesterol depletion and restoration on the human voltage-gated proton channel, hH_V1, in excised patches but negligible effects in the whole-cell configuration. Despite the presence of a putative cholesterol-binding site, a CARC motif in hH_V1, mutation of this motif did not affect cholesterol effects. The murine H_V1 lacks a CARC sequence but displays similar cholesterol effects. These results argue against a direct effect of cholesterol on the H_V1 protein. However, the data are fully explainable if H_V1 preferentially associates with cholesterol-dependent lipid domains, or "rafts." The rafts would be expected to concentrate in the membrane/glass int

SUBMITTER: Ayuyan AG 

PROVIDER: S-EPMC11700364 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature