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ProteomicsQuantitative Phosphoproteomics Reveals Crosstalk Between Phosphorylation and O-GlcNAc in the DNA Damage Response Pathway
The modification of intracellular proteins by monosaccharides of O-linked linked β-N-acetylglucosamine (O-GlcNAc) is thought to mediate proteins by regulating protein phosphorylation, either by modifying and modulating protein kinases or by competing with phosphorylation for hydroxyl residues. To pr...
ORGANISM(S): Mus musculus (Mouse) 
2015-01-28 | PXD001153 | Pride
Mouse embryonic fibroblast Atm Ogt knockout 
ProteomicsDissecting the Molecular Crosstalk between O-GlcNAcylation and Phosphorylation via Quantitative Proteomics and Phosphoproteomics
In this study, we explored the cross-talk between phosphorylation and O-GlcNAcylation using the pancreatic ductal cell line PANC-1 as a model. Proteome and phosphoproteome changes were measured for cells treated with OSMI-1, a specific inhibitor to O-GlcNAc transferase (OGT) and Thiamet G, a specif...
ORGANISM(S): Homo sapiens (Human) 
2026-06-29 | PXD070284 | Pride
Phosphorylation crosstalk o-glcnac 
ProteomicsWriting and erasing O-GlcNAc on casein kinase 2 alpha alters the phosphoproteome
O-GlcNAc is an essential carbohydrate modification that intersects with phosphorylation signaling pathways via crosstalk on protein substrates or by direct modification of the kinases that write the phosphate modification. Casein kinase 2 alpha (CK2), the catalytic subunit of the ubiquitously expres...
ORGANISM(S): Homo sapiens (Human) 
2022-04-26 | PXD030466 | Pride
Ck2 Casein kinase 2 Phosphoproteomics O-glcnac 
UnknownO-GlcNAc has crosstalk with ADP-ribosylation via PARG.
Not available
S-EPMC10654028 | biostudies-literature
UnknownQuantitative phosphoproteomics reveals crosstalk between phosphorylation and O-GlcNAc in the DNA damage response pathway.
Not available
S-EPMC4564869 | biostudies-literature
ProteomicsO-GlcNAc crosstalks with ADP-ribosylation via PARG
O-GlcNAc glycosylation is a prevalent protein post-translational modification (PTM) that occurs intracellularly. Previous investigations have demonstrated that O-GlcNAcylation crosstalks with phosphorylation and ubiquitination, but it is unclear whether it interplays with other PTMs. Here we studied...
ORGANISM(S): Homo sapiens (Human) 
2024-01-26 | PXD041119 | Pride
Hepatocellular carcinoma Poly(adp-ribosyl)ation O-glcnacylation Parg C-myc 
ProteomicsRegulation of Glycogen Synthase kinase 3beta by phosphorylation and O-beta-linked N-acetylglucosaminylation: implications on tau protein phosphorylation
Glycogen synthase kinase 3 (GSK3) plays a pivotal role in signaling pathways related to insulin metabolism and in the pathogenesis of Alzheimer s disease (AD) and other neurodegenerative disorders. More particularly, the GSK3beta isoform is involved in AD-associated tau pathology as one of the major...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2024-02-09 | MSV000094049 | MassIVE
UnknownThe O-GlcNAc Modification on Kinases.
Not available
S-EPMC7253032 | biostudies-literature
ProteomicsMapping and quantification of over 2,000 O-linked glycopeptides in activated human T cells with isotope-targeted glycoproteomics
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 o...
ORGANISM(S): Homo sapiens (Human) 
2018-01-25 | PXD004559 | Pride
Glycoproteomics Mass spectrometry O-glcnac T cells O-linked n-acetylglucosamine 
UnknownWriting and Erasing O-GlcNAc on Casein Kinase 2 Alpha Alters the Phosphoproteome.
Not available
S-EPMC9647470 | biostudies-literature
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