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PXD028141

PXD028141 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleTruncation of the TPR domain of OGT alters substrate and glycosite selection
DescriptionNucleocytoplasmic O-linked N-acetylglucosamine (O-GlcNAc) is an essential post-translational modification that is installed to thousands of protein substrates by O-GlcNAc transferase (OGT). Substrate selection by OGT and its isoforms is primarily mediated by the tetratricopeptide repeat (TPR) domain, yet the impact of truncations to the TPR domain on substrate and glycosite selection remains unresolved. Here, we report the effects of TPR truncations on the substrate and glycosite selection of OGT against the model protein GFP-JunB and the surrounding O-GlcNAc proteome in U2OS cells. Truncation of the TPR domain of OGT maintains glycosyltransferase activity but alters subcellular localization in cells. Examination of the glycoproteome across the TPR truncations revealed the broadest substrate activity from the canonical nucleocytoplasmic OGT, with the greatest changes in O-GlcNAc occurring on proteins associated with mRNA splicing processes. Glycosite analysis revealed alterations to the O-GlcNAc consensus sequence globally and differential glycosite selectivity on GFP-JunB as a function of the OGT TPR isoform. This dataset provides a foundation to analyze how perturbations to the TPR domain and expression of OGT isoforms affects the glycosylation of substrates, which will be critical for future protein engineering of OGT, the biology of OGT isoforms, and diseases associated with the TPR domain of OGT.
HostingRepositoryPRIDE
AnnounceDate2024-10-07
AnnouncementXMLSubmission_2024-10-07_10:55:56.352.xml
DigitalObjectIdentifierhttps://dx.doi.org/10.6019/PXD028141
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterChristina Woo
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListTMT6plex-126 reporter+balance reagent acylated residue; monohydroxylated residue; iodoacetic acid derivatized residue
InstrumentOrbitrap Fusion Lumos
Dataset History
RevisionDatetimeStatusChangeLog Entry
02021-08-26 04:05:34ID requested
12024-10-07 10:55:56announced
Publication List
10.6019/PXD028141;
Keyword List
submitter keyword: OGT, glycoproteomics, tetratricopeptide repeats (TPRs),O-GlcNAc
Contact List
Christina Woo
contact affiliationDEPARTMENT of CHEMISTRY & CHEMICAL BIOLOGY HARVARD UNIVERSITY
contact emailcwoo@chemistry.harvard.edu
lab head
Christina Woo
contact affiliationHarvard University
contact emailcwoo@chemistry.harvard.edu
dataset submitter
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