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Corrigendum: Lysine Acetylation and Succinylation in HeLa Cells and their Essential Roles in Response to UV-induced Stress

Authors :
Liangyan Wang
Kaiying Cheng
Xiaoli Xu
Xuanyi Chen
Shasha Suo
Meixia Wang
Ye Zhao
Bing Tian
Rongyi Shi
Zhiguo Zheng
Yuejin Hua
Hong Xu
Source :
Scientific Reports
Publication Year :
2017

Abstract

Lysine acetylation and succinylation are major types of protein acylation that are important in many cellular processes including gene transcription, cellular metabolism, DNA damage response. Malfunctions in these post-translational modifications are associated with genome instability and disease in higher organisms. In this study, we used high-resolution nano liquid chromatography-tandem mass spectrometry combined with affinity purification to quantify the dynamic changes of protein acetylation and succinylation in response to ultraviolet (UV)-induced cell stress. A total of 3345 acetylation sites in 1440 proteins and 567 succinylation sites in 246 proteins were identified, many of which have not been reported previously. Bioinformatics analysis revealed that these proteins are involved in many important biological processes, including cell signalling transduction, protein localization and cell metabolism. Crosstalk analysis between these two modifications indicated that modification switches might regulate protein function in response to UV-induced DNA damage. We further illustrated that FEN1 acetylation at different sites could lead to different cellular phenotypes, suggesting the multiple function involvement of FEN1 acetylation under DNA damage stress. These systematic analyses provided valuable resources and new insight into the potential role of lysine acetylation and succinylation under physiological and pathological conditions.

Details

ISSN :
20452322
Volume :
7
Database :
OpenAIRE
Journal :
Scientific reports
Accession number :
edsair.doi.dedup.....e684625af62133d1e8bce98ae0ccc233