Journal of Biological Chemistry
Volume 295, Issue 49, 4 December 2020, Pages 16497-16498
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Cutting out the fat: Site-specific deacylation of an ion channel

https://doi.org/10.1074/jbc.H120.016490Get rights and content
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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.

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Conflict of interest—The authors declare that they have no conflicts of interest with the contents of this article.

Abbreviations—The abbreviations used are:

    PTM

    post-translational modification

    STREX

    spliced stress-regulated exon

    LYPLA

    lysophospholipase

    zDHHC

    zinc-finger acyltransferase.