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...

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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
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author Kathayat, Rahul S.
Elvira, Pablo D.
Dickinson, Bryan C.
author_facet Kathayat, Rahul S.
Elvira, Pablo D.
Dickinson, Bryan C.
author_sort Kathayat, Rahul S.
collection PubMed
description 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.
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spelling pubmed-52473522017-06-19 A fluorescent probe for cysteine depalmitoylation reveals dynamic APT signaling Kathayat, Rahul S. Elvira, Pablo D. Dickinson, Bryan C. Nat Chem Biol Article 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. 2016-12-19 2017-02 /pmc/articles/PMC5247352/ /pubmed/27992880 http://dx.doi.org/10.1038/nchembio.2262 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Kathayat, Rahul S.
Elvira, Pablo D.
Dickinson, Bryan C.
A fluorescent probe for cysteine depalmitoylation reveals dynamic APT signaling
title A fluorescent probe for cysteine depalmitoylation reveals dynamic APT signaling
title_full A fluorescent probe for cysteine depalmitoylation reveals dynamic APT signaling
title_fullStr A fluorescent probe for cysteine depalmitoylation reveals dynamic APT signaling
title_full_unstemmed A fluorescent probe for cysteine depalmitoylation reveals dynamic APT signaling
title_short A fluorescent probe for cysteine depalmitoylation reveals dynamic APT signaling
title_sort fluorescent probe for cysteine depalmitoylation reveals dynamic apt signaling
topic Article
url 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
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