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Issue 11, 2017
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Michael addition-based probes for ratiometric fluorescence imaging of protein S-depalmitoylases in live cells and tissues

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Abstract

The reversible modification of cysteine residues through thioester formation with palmitate (protein S-palmitoylation) is a prevalent chemical modification that regulates the function, localization, and stability of many proteins. Current methods for monitoring the “erasers” of S-palmitoylation, acyl-protein thioesterases (APTs), rely on destructive proteomic methods or “turn-on” probes, precluding deployment in heterogeneous samples such as primary tissues. To address these challenges, we present the design, synthesis, and biological evaluation of Ratiometric Depalmitoylation Probes (RDPs). RDPs respond to APTs with a robust ratiometric change in fluorescent signal both in vitro and in live cells. Moreover, RDPs can monitor endogenous APT activities in heterogeneous primary human tissues such as colon organoids, presaging the utility of these molecules in uncovering novel roles for APTs in metabolic regulation.

Graphical abstract: Michael addition-based probes for ratiometric fluorescence imaging of protein S-depalmitoylases in live cells and tissues

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Submitted
23 Jun 2017
Accepted
09 Sep 2017
First published
11 Sep 2017

This article is Open Access
All publication charges for this article have been paid for by the Royal Society of Chemistry

Chem. Sci., 2017,8, 7588-7592
Article type
Edge Article

Michael addition-based probes for ratiometric fluorescence imaging of protein S-depalmitoylases in live cells and tissues

Michael W. Beck, R. S. Kathayat, C. M. Cham, E. B. Chang and B. C. Dickinson, Chem. Sci., 2017, 8, 7588
DOI: 10.1039/C7SC02805A

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