期刊
MOLECULAR CELL
卷 69, 期 3, 页码 438-+出版社
CELL PRESS
DOI: 10.1016/j.molcel.2017.12.019
关键词
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资金
- British Heart Foundation [BHF RG/12/12/29872]
- European Research Council (ERC Advanced award) [339095]
- Medical Research Council [MR/L009684/1]
- Department of Health via the NIHR cBRC award
- NIHR BRC award
- Biotechnology and Biological Sciences Research Council [BB/C503646/1] Funding Source: researchfish
- British Heart Foundation [PG/10/98/28655, PG/15/26/31373, RG/12/12/29872, FS/14/1/30551, IG/16/2/32273, RG/17/16/33294, PG/13/13/30018, FS/11/45/28859] Funding Source: researchfish
- Medical Research Council [MR/L009684/1, G1000458, 998501, MR/K003232/1, G0600785, G0700320] Funding Source: researchfish
- MRC [G0600785, G1000458, G0700320, MR/L009684/1, MR/K003232/1] Funding Source: UKRI
- European Research Council (ERC) [339095] Funding Source: European Research Council (ERC)
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.
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