An electrostatic switch controls palmitoylation of the large conductance voltage- and calcium-activated potassium (BK) channel.

ABSTRACT: Protein palmitoylation is a major dynamic posttranslational regulator of protein function. However, mechanisms that control palmitoylation are poorly understood. In many proteins, palmitoylation occurs at cysteine residues juxtaposed to membrane-anchoring domains such as transmembrane helices, sites of irreversible lipid modification, or hydrophobic and/or polybasic domains. In particular, polybasic domains represent an attractive mechanism to dynamically control protein palmitoylation, as the function of these domains can be dramatically influenced by protein phosphorylation. Here we demonstrate that a polybasic domain immediately upstream of palmitoylated cysteine residues within an alternatively spliced insert in the C terminus of the large conductance calcium- and voltage-activated pot

SUBMITTER: Jeffries O 

PROVIDER: S-EPMC3256903 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature