Article
OGA mutant aberrantly hydrolyzes O-GlcNAc modification from PDLIM7 to modulate p53 and cytoskeleton in promoting cancer cell malignancy.
Proceedings of the National Academy of Sciences of the United States of America - 11 Jun 2024
Hu Chia-Wei, Wang Ao, Fan Dacheng, Worth Matthew, Chen Zhengwei, Huang Junfeng, Xie Jinshan, Macdonald John, Li Lingjun, Jiang Jiaoyang
Abstract excerpt
O-GlcNAcase (OGA) is the only human enzyme that catalyzes the hydrolysis (deglycosylation) of O-linked beta-N-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...
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