Nonsubstrate PI(4,5)P₂ interacts with the interdomain linker to control electrochemical coupling in voltage-sensing phosphatase (VSP).

ABSTRACT: Voltage-sensing phosphatase (VSP) comprises a voltage sensor domain (VSD) and a cytoplasmic catalytic region (CCR), achieving a unique electrochemical signal conversion. Previous studies suggest that phosphatidylinositol 4,5-bisphosphate (PI(4,5)P₂), a membrane phospholipid known to be critical for activities of diverse voltage-gated ion channels, associates with a linker connecting the VSD with the CCR of VSP and regulates VSD-CCR coupling. However, the details of PI(4,5)P₂ interaction with the linker of VSP remain elusive. Here, we exploit advantage of sensitivity of a fluorescent unnatural amino acid, 3-(6-acetylnaphthalen-2-ylamino)-2-aminopropanoic acid (Anap), to changes in local environment to study interaction between PI(4,5)P₂ and the linker of

SUBMITTER: Mizutani N 

PROVIDER: S-EPMC12337349 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature