Dataset Information

O-GlcNAcome of OGA stalk domain mutants

ABSTRACT: THe O-GlcNAcome of OGA stlka domain mutation R586A and cancer derived mutation S652F in T-REx HEK293 cells

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Kidney Cell

DISEASE(S): Disease Free

SUBMITTER: Chia-Wei Hu

LAB HEAD: Jiaoyang Jiang

PROVIDER: PXD039798 | Pride | 2025-01-22

REPOSITORIES: pride

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Dataset's files

Source:

			Action	DRS
	2018_05_03_OGAg1_F1_R1.raw	Raw
	2018_05_03_OGAg1_F1_R2.raw	Raw
	2018_05_03_OGAg1_F2_R1.raw	Raw
	2018_05_03_OGAg1_F2_R2.raw	Raw
	2018_05_03_OGAg1_F3_R1.raw	Raw

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Publications

OGA mutant aberrantly hydrolyzes O-GlcNAc modification from PDLIM7 to modulate p53 and cytoskeleton in promoting cancer cell malignancy.

Hu Chia-Wei CW Wang Ao A Fan Dacheng D Worth Matthew M Chen Zhengwei Z Huang Junfeng J Xie Jinshan J Macdonald John J Li Lingjun L Jiang Jiaoyang J

Proceedings of the National Academy of Sciences of the United States of America 20240605 24

O-GlcNAcase (OGA) is the only human enzyme that catalyzes the hydrolysis (deglycosylation) of O-linked beta-<i>N</i>-acetylglucosaminylation (O-GlcNAcylation) from numerous protein substrates. OGA has broad implications in many challenging diseases including cancer. However, its role in cell malignancy remains mostly unclear. Here, we report that a cancer-derived point mutation on the OGA's noncatalytic stalk domain aberrantly modulates OGA interactome and substrate deglycosylation toward a spec ...[more]

PMID: 38838015

Similar Datasets

Project description:Drosophila development is a complex and dynamic process regulated, in part, by members of the Polycomb (Pc), Trithorax (Trx) and Compass chromatin modifier complexes. O-GlcNAc Transferase (OGT/SXC) is essential for Pc repression suggesting that the O-GlcNAcylation of proteins plays a key role in regulating development. OGT transfers N-acetyl-D-glucosamine (GlcNAc) onto hydroxyl groups of serine or threonine residues of key transcriptional regulators using the nutrient-derived UDP-GlcNAc as a substrate, which is dynamically removed by O-GlcNAcase (OGA). We performed ChIP-chip and microarray analysis after OGT or OGA RNAi knockdown in Drosophila S2 cells and found that O-GlcNAc was elevated genome wide particularly at genes related to mitosis and cell cycle in OGA RNAi cells, but not at sites co-occupied by Pc member Pleiohomeotic (Pho), such as the Hox and NK homeobox gene clusters. Microarray analysis suggested that altered O-GlcNAc cycling perturbed the expression of genes associated with morphogenesis and cell cycle regulation. To examine the in vivo consequences of disturbed O-GlcNAc cycling in the whole animal, we produced a null allele of oga (ogadel.1) in Drosophila. Epigenetic activators including Trx group members Trithorax (Trx), Absent small or homeotic discs 1 (Ash1) and Compass member Set1 histone methyltransferases are O-GlcNAc modified in ogadel.1 mutants. ogadel.1 mutants displayed altered expression of a distinct set of cell cycle related genes in ovaries. Our results suggest that the loss of OGA could affect epigenetic machinery by accumulating O-GlcNAc on numerous chromatin factors including Trx, Ash1 and Set1 in Drosophila. We performed affymetrix tilingarray analysis after OGT or OGA RNAi knockdown in Drosophila S2 cells to find if that O-GlcNAc was elevated genome wide particularly at genes related to mitosis and cell cycle in OGA RNAi cells, but not at sites co-occupied by Pc member Pleiohomeotic (Pho), ------------------------------- This represents the gene expression component only