Evidence against Stable Protein S-Nitrosylation as a Widespread Mechanism of Post-translational Regulation

• DOI: 10.1016/j.molcel.2017.12.019
• Publication Date: 2018-01-18T22:06:45Z
• Authors: Kathryn Wolhuter; Harry J. Whitwell; Christopher H. Sw...; Joseph R. Burgoyne; John F. Timms; Philip Eaton
• Keywords: Nitrosation; S-Nitrosylation; Nitrosylation

S-nitrosation, commonly referred to as S-nitrosylation, is widely regarded a ubiquitous, stable post-translational modification that directly regulates many proteins. Such widespread role would appear be incompatible with the inherent lability of S-nitroso bond, especially its propensity rapidly react thiols generate disulfide bonds. As anticipated, we observed robust and protein S-nitrosation after exposing cells nitrosocysteine or lipopolysaccharide. Proteins detected using ascorbate-dependent biotin switch method are typically interpreted regulated by S-nitrosation. However, these S-nitrosated proteins shown predominantly comprise transient intermediates leading bond formation. These disulfides likely dominant end effectors resulting from elevations in nitrosating cellular nitric oxide species. We propose primarily serves intermediate Overall, conclude current held perception function significantly incorrect.