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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
Published on: December 27, 2016
Temporal Profiling of Peroxynitrite-Mediated Protein Nitration and Phosphorylation Using Proteomics Analysis
Yating Yao1,2, Shuang Wang3, Jingyi Li2
1State Key Laboratory of Metabolic Dysregulation & Prevention and Treatment of Esophageal Cancer, Tianjian Laboratory of Advanced Biomedical Sciences, Academy of Medical Sciences, Zhengzhou University, Zhengzhou 450052, China.
Abstract:
Peroxynitrite is capable of inducing protein nitration, which alters protein structure and interferes with signaling pathways dependent on phosphorylation. This study aims to investigate the effects of peroxynitrite-driven nitration and phosphorylation on proteins in HEK293T cells. Through label-free quantitative mass spectrometry, we successfully identified over 5,000 proteins from 0.5 μg of cell extracts collected at five different time intervals (0, 2, 15, 30, and 60 min) after exposure to peroxynitrite. We found that protein expression profiles from 2 to 60 min were distinct from those at 0 min. LC-MS/MS was also applied to quantify and map the nitration and phosphorylation sites. Analysis of protein nitration and phosphorylation revealed distinct temporal profiles, suggesting that nitration may contribute to the altered phosphorylation of the same protein or its interacting proteins. This study provides valuable insights for further mechanistic studies in peroxynitrite-related pathways.

