A fluorescent probe for cysteine depalmitoylation reveals dynamic APT signaling
December 19th, 2016 by Rahul S Kathayat
Nature Chemical Biology 13, 150 (2017). doi:10.1038/nchembio.2262
Authors: Rahul S Kathayat, Pablo D Elvira & Bryan C Dickinson
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.