S-Acylation controls functional coupling of BK channel pore-forming α-subunits and β1-subunits.

ABSTRACT: The properties and physiological function of pore-forming α-subunits of large conductance calcium- and voltage-activated potassium (BK) channels are potently modified by their functional coupling with regulatory subunits in many tissues. However, mechanisms that might control functional coupling are very poorly understood. Here we show that S-acylation, a dynamic post-translational lipid modification of proteins, of the intracellular S0-S1 loop of the BK channel pore-forming α-subunit controls functional coupling to regulatory β1-subunits. In HEK293 cells, α-subunits that cannot be S-acylated show attenuated cell surface expression, but expression was restored by co-expression with the β1-subunit. However, we also found that nonacylation of the S0-S1 loop reduces functional c

SUBMITTER: Duncan PJ 

PROVIDER: S-EPMC6690687 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature