MassIVE MSV000081704

Imported Reanalysis Dataset Public PXD005903

Integrated lysine acetylation stoichiometry and proteomics analysis in human cells

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Description

Lysine acetylation is a widespread posttranslational modification that targets a large number of biological pathways. Recent studies reveal that lysine acetylation sites exhibit mainly low stoichiometry. Here we explored three sample preparation methods, the use of detergents for the chemical acetylation reaction in combination with stable and efficient alkylating reagent, to analyze the stoichiometry of acetylation in three human cell lines. We identified and determined the acetylation occupancy in about 1500 protein in each cell line. Lysine acetylation is highly dynamic, we determined variations in the acetylation stoichiometry when nearby residues are phosphorylated. The stoichiometric analysis in combination with quantitative proteomics allowed us to better understand the role of this PTM in different cells. We found that high abundance of the deacetylase SIRT1 correlates with less acetylation occupancy and abundance of ribosomes, proteins involved in ribosome biogenesis, rRNA processing, among others. We confirmed through the inhibition of SIRT1 with EX-527, followed by quantitative proteomics and acetylation stoichiometry analyzes, the negative role of this deacetylase on transcription and translation pathways. In addition, we found that SIRT1 positively regulates several metabolic pathways. [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Lysine Acetylation ; SIRT1 ; Proteomics ; Stoichiometry ; Cancer cells ; Deacetylase inhibitor

Contact

Principal Investigators:
(in alphabetical order) 		Sergio Manuel Encarnaci�n-Guevara, Programa de Gen�mica Funcional de Procariontes, Centro de Ciencias Gen�micas-UNAM. Av. Universidad s/n, Col. Chamilpa, Cuernavaca, Morelos. CP 62210. M�xico., N/A
Submitting User: ccms

Publications

Gil J, Ramírez-Torres A, Chiappe D, Luna-Peñaloza J, Fernandez-Reyes FC, Arcos-Encarnación B, Contreras S, Encarnación-Guevara S.
Lysine acetylation stoichiometry and proteomics analyses reveal pathways regulated by sirtuin 1 in human cells.
J. Biol. Chem. 2017 Nov 3;292(44):18129-18144. Epub 2017 Sep 11.

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Distinct protein accessions are counted across all files submitted in the "Statistical Analysis of Quantified Analytes" category having a "Protein" column in this dataset.

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