Cutting out the fat: Site-specific deacylation of an ion channel

4Citations
Citations of this article
7Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

S-Acylation, a reversible post-translational lipid modification of proteins, controls the properties and function of various proteins, including ion channels. Large conductance Ca2+-activated potassium (BK) channels are S-acylated at two sites that impart distinct functional effects.Whereas the enzymes that attach lipid groups are known, the enzymes mediating lipid removal (i.e. deacylation) are largely unknown. Here, McClafferty et al. identify two enzymes, ABHD17a and ABHD17c, that excise BK channel lipid groups with remarkable precision. These findings lend insights into mechanisms that orchestrate the (de)acylation that fine-tunes ion channel function in physiology and disease.

Cite

CITATION STYLE

APA

Del Rivero Morfin, P. J., & Ben-Johny, M. (2020, December 4). Cutting out the fat: Site-specific deacylation of an ion channel. Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology Inc. https://doi.org/10.1074/jbc.H120.016490

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free