A multiplexed NMR-reporter approach to measure cellular kinase and phosphatase activities in real-time

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Item Type:	Article
Title:	A multiplexed NMR-reporter approach to measure cellular kinase and phosphatase activities in real-time
Creators Name:	Thongwichian, R., Kosten, J., Benary, U., Rose, H.M., Stuiver, M., Theillet, F.X., Dose, A., Koch, B., Yokoyama, H., Schwarzer, D., Wolf, J. and Selenko, P.
Abstract:	Cell signaling is governed by dynamic changes in kinase and phosphatase activities, which are difficult to assess with discontinuous readout methods. Here, we introduce an NMR-based reporter approach to directly identify active kinases and phosphatases in complex physiological environments such as cell lysates and to measure their individual activities in a semicontinuous fashion. Multiplexed NMR profiling of reporter phosphorylation states provides unique advantages for kinase inhibitor studies and reveals reversible modulations of cellular enzyme activities under different metabolic conditions.
Keywords:	Biomolecular Nuclear Magnetic Resonance, Enzyme Activation, K562 Cells, Phosphoric Monoester Hydrolases, Phosphotransferases, Protein Kinase Inhibitors, Structure-Activity Relationship, Time Factors
Source:	Journal of the American Chemical Society
ISSN:	0002-7863
Publisher:	American Chemical Society
Volume:	137
Number:	20
Page Range:	6468-6471
Date:	27 May 2015
Official Publication:	https://doi.org/10.1021/jacs.5b02987
PubMed:	View item in PubMed

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