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Cutting out the fat: Site-specific deacylation of an ion channel
Journal of Biological Chemistry ( IF 4.0 ) Pub Date : 2020-12-04 , DOI: 10.1074/jbc.h120.016490
Pedro J Del Rivero Morfin 1 , Manu Ben-Johny 1
Affiliation  

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.

中文翻译:

消除脂肪:离子通道的位点特异性脱酰化

S-酰化是蛋白质的可逆翻译后脂质修饰,控制各种蛋白质(包括离子通道)的特性和功能。大电导 Ca2+ 激活钾 (BK) 通道在两个位点被 S 酰化,从而产生不同的功能效应。虽然连接脂质基团的酶是已知的,但介导脂质去除(即脱酰化)的酶在很大程度上是未知的。在这里,麦克拉弗蒂等人。鉴定出两种酶 ABHD17a 和 ABHD17c,它们能够以极高的精度切除 BK 通道脂质基团。这些发现有助于深入了解协调(去)酰化的机制,从而微调生理和疾病中的离子通道功能。
更新日期:2020-12-04
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