Proteomics

Dataset Information

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Nuclear phosphoproteomics analysis of resting and IL-2-stimulated T lymphocytes


ABSTRACT: 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.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): T Cell

DISEASE(S): Acute Leukemia

SUBMITTER: Nerea Osinalde  

LAB HEAD: Irina Kratchmarova

PROVIDER: PXD002839 | Pride | 2016-04-18

REPOSITORIES: Pride

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Publications

Nuclear Phosphoproteomic Screen Uncovers ACLY as Mediator of IL-2-induced Proliferation of CD4+ T lymphocytes.

Osinalde Nerea N   Mitxelena Jone J   Sánchez-Quiles Virginia V   Akimov Vyacheslav V   Aloria Kerman K   Arizmendi Jesus M JM   Zubiaga Ana M AM   Blagoev Blagoy B   Kratchmarova Irina I  

Molecular & cellular proteomics : MCP 20160411 6


Anti-cancer immunotherapies commonly rely on the use of interleukin-2 (IL-2) to promote the expansion of T lymphocytes. IL-2- dependent proliferation is the culmination of a complex network of phosphorylation-driven signaling events that impact on gene transcription through mechanisms that are not clearly understood. To study the role of IL-2 in the regulation of nuclear protein function we have performed an unbiased mass spectrometry-based study of the nuclear phosphoproteome of resting and IL-  ...[more]

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