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

O-GlcNAcase (OGA) is the only human enzyme that catalyzes the hydrolysis (deglycosylation) of O-linked beta- -acetylglucosaminylation (O-GlcNAcylation) from numerous protein substrates. OGA has broad implications in many challenging diseases including cancer. However, its role in cell malignancy rem...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2024-06, Vol.121 (24), p.e2320867121
Hauptverfasser:	Hu, Chia-Wei, Wang, Ao, Fan, Dacheng, Worth, Matthew, Chen, Zhengwei, Huang, Junfeng, Xie, Jinshan, Macdonald, John, Li, Lingjun, Jiang, Jiaoyang
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetylglucosamine - metabolism Actin Antigens, Neoplasm Biodegradation Biological Sciences Cancer Cell Line, Tumor Cell Movement Cell surface Complex formation Cytoskeleton Cytoskeleton - metabolism Deglycosylation Gene expression Glycosylation Histone Acetyltransferases Humans Hyaluronoglucosaminidase Hydrolysis LIM Domain Proteins - genetics LIM Domain Proteins - metabolism Malignancy MDM2 protein Mutants Mutation Neoplasms - genetics Neoplasms - metabolism Neoplasms - pathology O-GlcNAcylation p53 Protein Point mutation Proteins Proteomics Substrates Tumor suppressor genes Tumor Suppressor Protein p53 - genetics Tumor Suppressor Protein p53 - metabolism Ubiquitin-protein ligase
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