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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Cell Survival
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Cysteine / chemistry*
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Cysteine / metabolism*
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Fluorescent Dyes / analysis*
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Fluorescent Dyes / chemical synthesis
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Fluorescent Dyes / chemistry
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Humans
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Molecular Structure
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Signal Transduction*
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Thiolester Hydrolases / metabolism*
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Tumor Cells, Cultured
Substances
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Fluorescent Dyes
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Thiolester Hydrolases
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Cysteine
Associated data
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PubChem-Substance/319494456
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PubChem-Substance/319494457
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PubChem-Substance/319494458
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PubChem-Substance/319494459
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PubChem-Substance/319494460
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PubChem-Substance/319494461
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PubChem-Substance/319494462
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PubChem-Substance/319494463