
Research Square (Research Square), Journal Year: 2024, Volume and Issue: unknown
Published: Nov. 11, 2024
Language: Английский
Research Square (Research Square), Journal Year: 2024, Volume and Issue: unknown
Published: Nov. 11, 2024
Language: Английский
Cancer Letters, Journal Year: 2024, Volume and Issue: 588, P. 216742 - 216742
Published: Feb. 23, 2024
Language: Английский
Citations
11Nature Chemical Biology, Journal Year: 2025, Volume and Issue: unknown
Published: Jan. 7, 2025
Language: Английский
Citations
1Nature Metabolism, Journal Year: 2025, Volume and Issue: unknown
Published: March 17, 2025
Language: Английский
Citations
1Trends in Cell Biology, Journal Year: 2024, Volume and Issue: unknown
Published: Feb. 1, 2024
Language: Английский
Citations
5Journal of Biological Chemistry, Journal Year: 2024, Volume and Issue: 300(9), P. 107635 - 107635
Published: Aug. 5, 2024
Language: Английский
Citations
4Oncogenesis, Journal Year: 2025, Volume and Issue: 14(1)
Published: April 22, 2025
Fructose-1,6-bisphosphatase 1 (FBP1), a rate-limiting enzyme in gluconeogenesis, is important for cancer progression. The post-translational regulation of FBP1 hypoxic environments still unclear. Here, we report that down-regulated, and low expression level predicts poor prognosis pancreatic cancer. A environment makes more prone to degradation, this effect can be reversed by inhibiting global O-GlcNAcylation signalling. O-linked N-acetylglucosamine transferase (OGT) interacts with induces its at serine 47 residue (FBP1-S47) modulate protein function cells. FBP1-S47 promotes degradation also influences the canonical HIF-1α target genes involved glucose metabolism, resulting an increase uptake lactate secretion In addition, facilitates K48-linked polyubiquitination lysine 51 (FBP1-K51), which GlcNAc moiety serve as prerequisite ubiquitin ligase. (K51) mediated promote progression, similarly FBP1-S47. Our data uncover mechanism whereby regulated O-GlcNAcylation-polyubiquitination axis, paving way cell metabolic reprogramming.
Language: Английский
Citations
0Journal of genetics and genomics/Journal of Genetics and Genomics, Journal Year: 2025, Volume and Issue: unknown
Published: April 1, 2025
Language: Английский
Citations
0Biomolecules, Journal Year: 2024, Volume and Issue: 14(8), P. 908 - 908
Published: July 25, 2024
Post-translational modifications (PTMs) influence protein functionality by modulating stability, localization, and interactions with other molecules, thereby controlling various cellular processes. Common PTMs include phosphorylation, acetylation, ubiquitination, glycosylation, SUMOylation, methylation, sulfation, nitrosylation. Among these modifications, O-GlcNAcylation has been shown to play a critical role in cancer development progression, especially hepatocellular carcinoma (HCC). This review outlines the of progression HCC. Moreover, we delve into underlying mechanisms HCC highlight compounds that target O-GlcNAc transferase (OGT) O-GlcNAcase (OGA) improve treatment outcomes. Understanding will offer insights potential therapeutic strategies targeting OGT OGA, which could for patients
Language: Английский
Citations
3Developmental Cell, Journal Year: 2025, Volume and Issue: 60(7), P. 994 - 1007
Published: April 1, 2025
Language: Английский
Citations
0Analytical and Bioanalytical Chemistry, Journal Year: 2024, Volume and Issue: unknown
Published: Sept. 18, 2024
Language: Английский
Citations
2