A fluorescent probe for cysteine depalmitoylation reveals dynamic APT signaling.

A fluorescent probe for cysteine depalmitoylation reveals dynamic APT signaling.
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半胱氨酸二光二酰化的荧光探针揭示了动态的APT信号传导。

DOI:
10.1038/nchembio.2262
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发表时间:
2017-02
影响因子:
14.8
通讯作者:
Dickinson BC
Dickinson BC
中科院分区:
生物学1区
文献类型:
--
作者:
Kathayat RS;Elvira PD;Dickinson BC

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数百种人类蛋白质通过半胱氨酸残基的可逆棕榈酰化(S-棕榈酰化)进行修饰,但对脱棕榈酰化的调控知之甚少。在这里,我们开发了“脱棕榈酰化探针”(DPP),小分子荧光团,以监测内源性活性水平的“橡皮擦”的S-棕榈酰化,酰基蛋白硫酯酶(APT)。DPP的活细胞分析揭示了快速生长因子介导的APTs脱棕榈酰化活性的抑制,揭示了动态脂质信号传导的新调控机制。
Hundreds of human proteins are modified by reversible palmitoylation of cysteine residues (S-palmitoylation), but the regulation of depalmitoylation is poorly understood. Here, we develop “depalmitoylation probes” (DPPs), small molecule fluorophores to monitor the endogenous activity levels of “erasers” of S-palmitoylation, acyl-protein thioesterases (APTs). Live-cell analysis with DPPs reveals rapid growth factor-mediated inhibition of the depalmitoylation activity of APTs, exposing a novel regulatory mechanism of dynamic lipid signaling.