Protein lysine acetylation analysis: current MS-based proteomic technologies.
Protein lysine acetylation (Kac), including histone acetylation and non-nuclear protein acetylation, is a dynamic and reversible post-translational modification for cellular regulation. The modified proteins play a key role in regulating chromatin structure, transcriptional activity and metabolic pathways, thus contributing to diverse cellular processes like transcription, cell cycle regulation, apoptosis and senescence. Therefore, targeting protein acetylation represents a potentially promising strategy for certain diseases, such as cancer. However, global identification of protein acetylation is a major bottleneck due to its dynamic property and rather low abundance. Tremendous efforts have been made to develop mass spectrometry (MS)-based proteomic technologies for this purpose from diverse cellular sources. The present review has tried to provide an overview of current strategies employed for Kac identification from histone to system-wide Kac analysis, including enrichment techniques, chromatographic separation strategies, and mass spectrometry methods.
State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin 300071, China. Zhangkai730@yahoo.com.cn
Kai
K
Zhang
Shanshan
S
Tian
Enguo
E
Fan
D000107:Acetylation; D000818:Animals; D006801:Humans; D008239:Lysine / Q000737:chemistry* / Q000378:metabolism; D013058:Mass Spectrometry / Q000379:methods*; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D040901:Proteomics / Q000379:methods*
D011506:Proteins; D008239:Lysine