A phosphoproteomics view at human pluripotent stem cells

Abstract

Reversible protein phosphorylation has been one of the most investigated post-translational modifications (PTM) in the decade, made possible by advances in enrichment technologies and MS-based proteomics. PTMs are generally involved in the regulation of many biological processes, including processes that regulate pluripotency and self-renewal of stem cells. In recent years, several enrichment methods have been introduced that helped to improve the detection and quantitation of phosphorylated peptides by MS enabling the study of phosphorylation dynamics in cells and tissues. The work described in this thesis is focused on the application of a selection of such proteomic strategies, for the investigation of phosphorylation events in pluripotent stem cells.