PXD010155

PXD010155 is an original dataset announced via ProteomeXchange.

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

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.

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;

curator keyword: Biological

submitter keyword: Inducible expression, GalNAc-transferase, O-glycosylation, glycoproteomics, mass spectrometry

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

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PRIDE project URI

• PRIDE
  1. PXD010155
     1. Label: PRIDE project
     2. Name: Probing the contribution of individual polypeptide GalNAc-transferase isoforms to the O-glycoproteome by inducible expression in isogenic cell lines