PXD004559 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Mapping and quantification of over 2,000 O-linked glycopeptides in activated human T cells with isotope-targeted glycoproteomics |
Description | Post-translational modifications (PTMs) on proteins often function to regulate signaling cascades, with the activation of T cells during an adaptive immune response being a classic example. Mounting evidence indicates that the modification of proteins by O-linked Nacetylglucosamine (O-GlcNAc), the only mammalian glycan found on nuclear and cytoplasmic proteins, helps regulate T cell activation. Yet, a mechanistic understanding of how O-GlcNAc functions in T cell activation remains elusive, partly because of the difficulties in mapping and quantifying O-GlcNAc sites. Thus, to advance insight into the role of O-GlcNAc in T cell activation, we performed extensive glycosite mapping studies via direct glycopeptide measurement on resting and activated primary human T cells with a technique termed isotope targeted glycoproteomics. This approach led to the identification of over 2,000 intact O-GlcNAccontaining glycopeptides across 1,046 glycoproteins. A significant proportion (>45%) of the identified O-GlcNAc sites lie in close proximity to or coincide with known phosphorylation sites, supporting the potential for PTM crosstalk. Consistent with other studies, we find that O-GlcNAc sites in T cells lack a strict consensus sequence. To validate our results, we employed gel shift assays based on conjugating mass tags to O-GlcNAc groups. Notably, we observed that the transcription factors c-JUN and JUNB show higher levels of O-GlcNAc glycosylation and higher levels of expression in activated T cells. Overall, our findings provide a quantitative characterization of O-GlcNAc glycoproteins and their corresponding modification sites in primary human T cells, which will facilitate mechanistic studies into the function of O-GlcNAc in T cell activation. |
HostingRepository | PRIDE |
AnnounceDate | 2018-01-25 |
AnnouncementXML | Submission_2018-01-25_01:24:47.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Christina Woo |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | N-acetylaminoglucosylated |
Instrument | LTQ Orbitrap Elite |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2016-07-12 01:59:22 | ID requested | |
⏵ 1 | 2018-01-25 01:24:48 | announced | |
Publication List
Woo CM, Lund PJ, Huang AC, Davis MM, Bertozzi CR, Pitteri SJ, Mapping and Quantification of Over 2000 O-linked Glycopeptides in Activated Human T Cells with Isotope-Targeted Glycoproteomics (Isotag). Mol Cell Proteomics, 17(4):764-775(2018) [pubmed] |
Keyword List
submitter keyword: O-linked N-acetylglucosamine, O-GlcNAc, glycoproteomics, T cells, mass spectrometry |
Contact List
Christina Woo |
contact affiliation | Department of Chemistry and Chemical Biology Harvard University |
contact email | cwoo@chemistry.harvard.edu |
lab head | |
Christina Woo |
contact affiliation | Harvard University |
contact email | cwoo@chemistry.harvard.edu |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD004559
- Label: PRIDE project
- Name: Mapping and quantification of over 2,000 O-linked glycopeptides in activated human T cells with isotope-targeted glycoproteomics