A fluorescent probe for cysteine depalmitoylation reveals dynamic APT signaling

Nat Chem Biol. 2017 Feb;13(2):150-152. doi: 10.1038/nchembio.2262. Epub 2016 Dec 19.

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

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Survival
  • Cysteine / chemistry*
  • Cysteine / metabolism*
  • Fluorescent Dyes / analysis*
  • Fluorescent Dyes / chemical synthesis
  • Fluorescent Dyes / chemistry
  • Humans
  • Molecular Structure
  • Signal Transduction*
  • Thiolester Hydrolases / metabolism*
  • Tumor Cells, Cultured

Substances

  • Fluorescent Dyes
  • Thiolester Hydrolases
  • Cysteine

Associated data

  • PubChem-Substance/319494456
  • PubChem-Substance/319494457
  • PubChem-Substance/319494458
  • PubChem-Substance/319494459
  • PubChem-Substance/319494460
  • PubChem-Substance/319494461
  • PubChem-Substance/319494462
  • PubChem-Substance/319494463