The aim of the present project was to study in detail the site-specific phosphorylation events occurring both in resting as well as in T lymphocytes stimulated with IL-2 for five minutes. For that purpose we combined SILAC-based quantitative mass spectrometry analysis with phosphopeptide enrichment using TiO2 beads. We performed three biological replicas of the same experiment which resulted in the identification of above 8500 unique phosphosites corresponding to more than 3000 proteins. From the 6145 phosphosites that were consistently quantified in at least 2 out of the 3 replicas performed, we detected that 390 were regulated by IL-2 being the up-regulated phosphosites five times more abundant than the down-regulated ones. Those IL-2-dependent phosphosites corresponded to distinct proteins involved in distinct aspects of gene expression and cell cycle regulation.
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: Phosphorylation ; IL-2 ; T-lymphocyte ; nucleus
Principal Investigators: (in alphabetical order) |
Irina Kratchmarova, Associate Professor Department of Biochemistry and Molecular Biology University of Southern Denmark Campusvej 55, 5230 Odense M Denmark e-mail: ihk@bmb.sdu.dk Phone: (+45) 6550 2494 Fax: (+45) 6593 3018 http://www.cebi.sdu.dk, N/A |
Submitting User: | ccms |
Osinalde N, Mitxelena J, Sánchez-Quiles V, Akimov V, Aloria K, Arizmendi JM, Zubiaga AM, Blagoev B, Kratchmarova I.
Nuclear Phosphoproteomic Screen Uncovers ACLY as Mediator of IL-2-induced Proliferation of CD4+ T lymphocytes.
Mol. Cell Proteomics. 2016 Jun;15(6):2076-92. Epub 2016 Apr 11.
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