Data on interleukin (IL)-2- and IL-15-dependent changes in IL-2Rβand IL-2Rγ complexes.
We provide detailed datasets from our analysis of the proteins that associate with IL-2Rβ and IL-2Rγ in T-cells stimulated with IL-2 or IL-15 compared with resting T-cells, as identified by SILAC-based quantitative proteomics. We also include quantitative data regarding site-specific phosphorylation events observed both in IL-2Rβ and IL-2Rγ. Moreover, we provide results demonstrating the specific protein recruitment capacity of four of those site-specific phosphorylations. The proteomics and phosphoproteomics data described in this article is associated with a research article entitled "Characterization of receptor-associated protein complex assembly in Interleukin (IL)-2- and IL-15-activated T-lymphocytes" (Osinalde et al., 2016 [1]). The mass spectrometry data have been deposited to the ProteomeEXchange Constorium with the identifier PXD002386.
Department of Biochemistry and Molecular Biology, University of the Basque Country UPV/EHU, 01006 Vitoria-Gasteiz, Spain.
Nerea
N
Osinalde
Molecular Oncology Group, UMR 144 CNRS, Curie Institute, 26, rue d'Ulm, 75248 Paris, France.
Virginia
V
Sánchez-Quiles
Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense M, Denmark.
Blagoy
B
Blagoev
Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense M, Denmark.
Irina
I
Kratchmarova
Cell signaling; Interactome; Interleukin; Phosphotyrosine; SILAC; T-lymphocytes