Abstract
The p53 tumor suppressor protein is a key regulator of cell cycle and death that is involved in many cell signaling pathways and is tightly regulated in mammalian cells. Post-translational modifications of p53 have been investigated previously mainly using antibodies. In this study, utilizing LC-MS/MS analysis, we have characterized p53 protein from COS-1 cells. Several already known post-translational modifications were observed, such as phosphorylation on serines 15, 33, 315, and 392 as well as acetylation on lysines 305, 370, 372, 373, 381, 382, and 386. Interestingly novel acetylation sites were identified at lysines 319 and 357. This study confirmed that p53 is a highly acetylated protein and revealed new acetylation sites that might aid the further understanding of p53 regulation.
Highlights
The p53 tumor suppressor protein is a key regulator of cell cycle and death that is involved in many cell signaling pathways and is tightly regulated in mammalian cells
Sequencing of p53 Protein in COS-1 Cells—p53 was immunoprecipitated from COS-1 cells
We have identified phosphorylation and acetylation sites on endogenous p53 from COS-1 cells
Summary
The p53 tumor suppressor protein is a key regulator of cell cycle and death that is involved in many cell signaling pathways and is tightly regulated in mammalian cells. Because of its central function in processes such as cell cycle regulation, apoptosis, DNA repair, cellular senescence, and apoptosis, the p53 pathway is crucial for effective tumor suppression, and mutations in p53 that compromise its function occur in more than 50% of cancers [1, 2]. P53 appears to be highly posttranslationally modified, and ubiquitination, neddylation, sumoylation, and methylation have been described, phosphorylation and acetylation are the most commonly reported modifications of p53 [3]. Both phosphorylation and acetylation affect p53 stability and activity and are induced following various types of stress [4]. Functional proteomics,” University Lille 1, 59655 Villeneuve d’Ascq, France
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