title: 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.
authors.affiliation: Department of Chemistry, University of Chicago, Chicago, Illinois, USA.
authors.forename: Rahul S
authors.initials: RS
authors.lastname: Kathayat
authors.affiliation: Department of Chemistry, University of Chicago, Chicago, Illinois, USA.
authors.forename: Pablo D
authors.initials: PD
authors.lastname: Elvira
authors.affiliation: Department of Chemistry, University of Chicago, Chicago, Illinois, USA.
authors.forename: Bryan C
authors.initials: BC
authors.lastname: Dickinson
mesh_terms: D002470:Cell Survival; D003545:Cysteine / Q000737:chemistry* / Q000378:metabolism*; D005456:Fluorescent Dyes / Q000032:analysis* / Q000138:chemical synthesis / Q000737:chemistry; D006801:Humans; D015394:Molecular Structure; D015398:Signal Transduction; D013869:Thiolester Hydrolases / Q000378:metabolism*; D014407:Tumor Cells, Cultured
chemical_list: D005456:Fluorescent Dyes; D013869:Thiolester Hydrolases; D003545:Cysteine