A fluorescent probe for cysteine depalmitoylation reveals dynamic APT signaling

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 “eras...

Descripción completa

Detalles Bibliográficos
Autores principales: Kathayat, Rahul S., Elvira, Pablo D., Dickinson, Bryan C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2016
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5247352/
https://www.ncbi.nlm.nih.gov/pubmed/27992880
http://dx.doi.org/10.1038/nchembio.2262
Descripción
Sumario: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, acyl-protein 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.

Ejemplares similares