Dataset Information

Mus musculus primary CD4+ T cell di-glycine remnant and whole cell proteomics

ABSTRACT: It is known that ubiquitination is important for T cell receptor (TCR) signaling during T cell activation but the breadth of ubiquitination events triggered during TCR signaling is not completely understood. This dataset utilizes di-glycine remnant profiling combined with mass spectrometry to identify a global landscape of ubiquitination events downstream of the TCR and to quantify changes ubiquitin abundance in response to TCR stimulation. Additionally, whole cell proteomics data were generated to measure protein abundances during TCR stimulation. Mouse primary T cells were isolated, proliferated and either remained resting or stimulated with CD3/CD28 to activate downstream signaling through the TCR and co-stimulatory pathways. Di-glycine remnant profiling and whole cell proteomics was performed on rested cells and cells that had undergone CD3/CD28 TCR stimulation for 4 hours. These data were analyzed to identify the ubiquitination events during TCR activation and to quantify the change in peptide-based ubiquitin abundance and total protein abundance over the course of the 4 hour TCR stimulation. Integration of di-glycine and whole cell proteomics was used to generate protein-specific predictions of whether ubiquitination events downstream of TCR signaling lead to a decrease in associated protein abundance. The analysis of these data suggests that T cell activation leads to an increase in ubiquitination that is not associated with proteasomal or lysosomal degradation.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): T Cell

SUBMITTER: Hossein Fazelinia

LAB HEAD: Steven Seeholzer

PROVIDER: PXD012831 | Pride | 2019-05-09

REPOSITORIES: Pride

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			Action	DRS
	e150319_PO972kgg_0hr_2_02a.raw	Raw
	e150319_PO972kgg_0hr_2_02b.raw	Raw
	e150319_PO972kgg_0hr_2_04a.raw	Raw
	e150319_PO972kgg_0hr_2_04b.raw	Raw
	e150319_PO972kgg_0hr_3_01a.raw	Raw

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Publications

Integrative proteomics reveals an increase in non-degradative ubiquitylation in activated CD4<sup>+</sup> T cells.

Dybas Joseph M JM O'Leary Claire E CE Ding Hua H Spruce Lynn A LA Seeholzer Steven H SH Oliver Paula M PM

Nature immunology 20190506 6

Despite gathering evidence that ubiquitylation can direct non-degradative outcomes, most investigations of ubiquitylation in T cells have focused on degradation. Here, we integrated proteomic and transcriptomic datasets from primary mouse CD4<sup>+</sup> T cells to establish a framework for predicting degradative or non-degradative outcomes of ubiquitylation. Di-glycine remnant profiling was used to reveal ubiquitylated proteins, which in combination with whole-cell proteomic and transcriptomic ...[more]

PMID: 31061531

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