PXD010155 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Probing the contribution of individual polypeptide GalNAc-transferase isoforms to the O-glycoproteome by inducible expression in isogenic cell lines |
Description | The GalNAc-type O-glycoproteome is orchestrated by a large family of polypeptide GalNAc-transferase isoenzymes (GalNAc-Ts) with partially overlapping contributions to the O-glycoproteome as well as distinct non-redundant functions. Increasing evidence indicate that individual GalNAc-Ts co-regulate and fine-tune specific protein functions in health and disease, and deficiencies in individual GALNT genes underlie congenital diseases with distinct phenotypes. Studies of GalNAc-T specificities have mainly been performed with in vitro enzyme assays using short peptide substrate, but recently quantitative differential O-glycoproteomics of isogenic cells with and without GALNT genes has enabled a more unbiased exploration of the non-redundant contributions of individual GalNAc-Ts. Both approaches suggest that fairly small subsets of O-glycosites are non-redundantly regulated by specific GalNAc-Ts, but how these isoenzymes orchestrate regulation amongst competing redundant substrates is unclear. To explore this, we developed isogenic cell model systems with Tet-On inducible expression of two GalNAc-T genes, GALNT2 and GALNT11, in a knockout background. Using quantitative O-glycoproteomics with TMT labelling we found that isoform-specific glycosites were glycosylated in a dose dependent manner, and induction of GalNAc-T2 or T11 produced discrete glycosylation effects without affecting the major part of the glycoproteome. The results support the findings that individual GalNAc-T isoenzymes can serve in fine-tuned regulation of distinct protein functions |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_04:45:46.028.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Sergey Vakhrushev |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | TMT6plex-126 reporter+balance reagent acylated residue; monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | LTQ Orbitrap |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2018-06-18 08:44:16 | ID requested | |
1 | 2018-10-16 09:08:21 | announced | |
2 | 2018-10-22 06:21:13 | announced | Updated publication reference for PubMed record(s): 30327431. |
⏵ 3 | 2024-10-22 04:45:52 | announced | 2024-10-22: Updated project metadata. |
Publication List
Hintze J, Ye Z, Narimatsu Y, Madsen TD, Joshi HJ, Goth CK, Linstedt A, Bachert C, Mandel U, Bennett EP, Vakhrushev SY, Schjoldager KT, -glycoproteome by inducible expression in isogenic cell lines. J Biol Chem, 293(49):19064-19077(2018) [pubmed] |
10.1074/jbc.ra118.004516; |
Keyword List
curator keyword: Biological |
submitter keyword: Inducible expression, GalNAc-transferase, O-glycosylation, glycoproteomics, mass spectrometry |
Contact List
Sergey Vakhrushev |
contact affiliation | Associate Professor Glyco MS Group Copenhagen Center for Glycomics (CCG) Department of Cellular and Molecular Medicine University of Copenahgen Blegdamsvej 3 2200 Copenhagen N Denmark |
contact email | seva@sund.ku.dk |
lab head | |
Sergey Vakhrushev |
contact affiliation | Department of Cellular and Molecular Medicine |
contact email | seva@sund.ku.dk |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD010155
- Label: PRIDE project
- Name: Probing the contribution of individual polypeptide GalNAc-transferase isoforms to the O-glycoproteome by inducible expression in isogenic cell lines