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A fluorescent probe for cysteine depalmitoylation reveals dynamic APT signaling.

ABSTRACT: 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, acylprotein 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.

SUBMITTER: Kathayat RS

PROVIDER: S-EPMC5247352 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature

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A fluorescent probe for cysteine depalmitoylation reveals dynamic APT signaling.

Kathayat Rahul S RS Elvira Pablo D PD Dickinson Bryan C BC

Nature chemical biology 20161219 2

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, acylprotein thioesterases (APTs). Live-cell analysis with DPPs reveals rapid growth-factor-mediated inhibition of the depalmitoylation activity of APTs, exposing a novel reg ...[more]

PMID: 27992880

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