Cutting out the fat: Site-specific deacylation of an ion channel.
Cutting out the fat: Site-specific deacylation of an ion channel.
复制标题
减少脂肪：离子通道的位点特异性脱酰化。
DOI：
10.1074/jbc.h120.016490
复制
发表时间：
2020-12-04
期刊：
影响因子：
--
通讯作者：
Ben-Johny M
中科院分区：
文献类型：
--
作者：
Del Rivero Morfin PJ;Ben-Johny M
S酰化是蛋白质可逆的翻译后脂质修饰，控制着包括离子通道在内的各种蛋白质的性质和功能。大电导钙激活钾(BK)通道在两个位点被S酰化，具有不同的功能效应。虽然连接类脂基团的酶是已知的，但介导脱脂(即脱酰)的酶在很大程度上是未知的。这里，McClafferty等人。鉴定两种酶，ABHD17a和ABHD17c，它们以惊人的精度去除BK通道类脂基团。这些发现有助于深入了解协调(去)酰化的机制，该机制微调生理和疾病中的离子通道功能。
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.