Imperial College London
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DrHarryWhitwell

Faculty of Medicine, Department of Metabolism, Digestion and Reproduction

Lecturer in Proteomics and Integrative Data Analysis Proteom
 
 
 
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Location

 

312Burlington DanesHammersmith Campus

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Summary

 

Publications

Citation

BibTex format

@article{Wolhuter:2018:10.1016/j.molcel.2017.12.019,
author = {Wolhuter, K and Whitwell, HJ and Switzer, CH and Burgoyne, JR and Timms, JF and Eaton, P},
doi = {10.1016/j.molcel.2017.12.019},
journal = {MOLECULAR CELL},
pages = {438--450.e5},
title = {Evidence against Stable Protein S-Nitrosylation as a Widespread Mechanism of Post-translational Regulation},
url = {http://dx.doi.org/10.1016/j.molcel.2017.12.019},
volume = {69},
year = {2018}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - S-nitrosation, commonly referred to as S-nitrosylation, is widely regarded as a ubiquitous, stable post-translational modification that directly regulates many proteins. Such a widespread role would appear to be incompatible with the inherent lability of the S-nitroso bond, especially its propensity to rapidly react with thiols to generate disulfide bonds. As anticipated, we observed robust and widespread protein S-nitrosation after exposing cells to nitrosocysteine or lipopolysaccharide. Proteins detected using the ascorbate-dependent biotin switch method are typically interpreted to be directly regulated by S-nitrosation. However, these S-nitrosated proteins are shown to predominantly comprise transient intermediates leading to disulfide bond formation. These disulfides are likely to be the dominant end effectors resulting from elevations in nitrosating cellular nitric oxide species. We propose that S-nitrosation primarily serves as a transient intermediate leading to disulfide formation. Overall, we conclude that the current widely held perception that stable S-nitrosation directly regulates the function of many proteins is significantly incorrect.
AU  - Wolhuter,K
AU  - Whitwell,HJ
AU  - Switzer,CH
AU  - Burgoyne,JR
AU  - Timms,JF
AU  - Eaton,P
DO  - 10.1016/j.molcel.2017.12.019
EP  - 450
PY  - 2018///
SN  - 1097-2765
SP  - 438
TI  - Evidence against Stable Protein S-Nitrosylation as a Widespread Mechanism of Post-translational Regulation
T2  - MOLECULAR CELL
UR  - http://dx.doi.org/10.1016/j.molcel.2017.12.019
UR  - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000423844800009&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR  - http://hdl.handle.net/10044/1/59244
VL  - 69
ER  -
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