Role of O-GlcNAcylation on cancer stem cells: Connecting nutrient sensing to cell plasticity

Minh, Giang Le; Reginato, Mauricio J.

doi:10.1016/bs.acr.2022.06.002

Cited by 5 publications

(2 citation statements)

References 189 publications

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“…In addition to miR-485-5p, miR-101 targets OGT-mediated O -GlcNAcylation, further inhibiting colorectal cancer progression [ 139 , 140 ]. MicroRNA24 is also an OGT regulator, reduces the O -GlcNAcylation of FOXA1 and c-Myc, and prevents breast cancer cells and mouse hepatoma cell invasion, respectively [ 141 , 142 ]. Moreover, miR-424-5p could target OGT, further inhibiting the progression of liver cancer and clear cell renal cell carcinoma [ 143 ].…”

Section: Small Molecules Targeting Ogtmentioning

confidence: 99%

Can O-GIcNAc Transferase (OGT) Complex Be Used as a Target for the Treatment of Hematological Malignancies?

Zhuang,

Liu,

et al. 2024

Pharmaceuticals

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The circulatory system is a closed conduit system throughout the body and consists of two parts as follows: the cardiovascular system and the lymphatic system. Hematological malignancies usually grow and multiply in the circulatory system, directly or indirectly affecting its function. These malignancies include multiple myeloma, leukemia, and lymphoma. O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) regulates the function and stability of substrate proteins through O-GlcNAc modification. Abnormally expressed OGT is strongly associated with tumorigenesis, including hematological malignancies, colorectal cancer, liver cancer, breast cancer, and prostate cancer. In cells, OGT can assemble with a variety of proteins to form complexes to exercise related biological functions, such as OGT/HCF-1, OGT/TET, NSL, and then regulate glucose metabolism, gene transcription, cell proliferation, and other biological processes, thus affecting the development of hematological malignancies. This review summarizes the complexes involved in the assembly of OGT in cells and the role of related OGT complexes in hematological malignancies. Unraveling the complex network regulated by the OGT complex will facilitate a better understanding of hematologic malignancy development and progression.

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Section: Small Molecules Targeting Ogtmentioning

confidence: 99%

Can O-GIcNAc Transferase (OGT) Complex Be Used as a Target for the Treatment of Hematological Malignancies?

Zhuang,

Liu,

et al. 2024

Pharmaceuticals

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“…It is catalyzed by the O-GlcNAc transferase (OGT) and removed by the O-GlcNAcase (OGA). Decades of glycobiology research have witnessed emerging chemical and biological tools (3,4) that have demonstrated that O-GlcNAc occurs on about 5 000 proteins and regulates tumorigenesis and immunotherapy (5), ferroptosis (6), protein aggregation and phase separation (7), stem cell biology (8), liver metabolism (9), neurodevelopment and various stress response pathways (10).…”

Section: Introductionmentioning

confidence: 99%

O-GlcNAcylation of YTHDF2 antagonizes ERK-dependent phosphorylation and inhibits lung carcinoma

Li,

Zhou,

Zhang

et al. 2023

Preprint

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SUMMARYThe intracellular O-linked N-acetylglucosamine (O-GlcNAc) glycosylation mediates many signal transduction events and regulates tumorigenesis. Previously the RNA N6-methyladenosine (m6A) reader, YTH (YT521-B homology) domain 2 (YTHDF2), has been shown to be O-GlcNAcylated on Ser-263 during Hepatitis B virus (HBV) infection and promote HBV-related hepatocellular carcinoma. Herein we mapped YTHDF2 O-GlcNAcylation at Thr-49 via electron-transfer dissociation mass spectrometry under unperturbed conditions. We show that YTHDF2 Thr-49 O-GlcNAcylation antagonizes Extracellular-signal regulated kinase (ERK)-dependent phosphorylation at Ser-39 and promotes YTHDF2 degradation. The downstream signaling pathway of YTHDF2 in lung carcinoma are thus upregulated, which leads to the downregulation of c-Myc. We further used mouse xenograft models to show that YTHDF2-T49A mutants increased lung cancer mass and size. Our work reveals a key role of YTHDF2 O-GlcNAcylation in tumorigenesis and suggests that O-GlcNAcylation exerts distinct functions under different biological stress.

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Altered glycosylation in cancer: molecular functions and therapeutic potential

Xu,

Peng,

Jiang

et al. 2024

Cancer Communications

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Glycosylation, a key mode of protein modification in living organisms, is critical in regulating various biological functions by influencing protein folding, transportation, and localization. Changes in glycosylation patterns are a significant feature of cancer, are associated with a range of pathological activities in cancer‐related processes, and serve as critical biomarkers providing new targets for cancer diagnosis and treatment. Glycoproteins like human epidermal growth factor receptor 2 (HER2) for breast cancer, alpha‐fetoprotein (AFP) for liver cancer, carcinoembryonic antigen (CEA) for colon cancer, and prostate‐specific antigen (PSA) for prostate cancer are all tumor biomarkers approved for clinical use. Here, we introduce the diversity of glycosylation structures and newly discovered glycosylation substrate—glycosylated RNA (glycoRNA). This article focuses primarily on tumor metastasis, immune evasion, metabolic reprogramming, aberrant ferroptosis responses, and cellular senescence to illustrate the role of glycosylation in cancer. Additionally, we summarize the clinical applications of protein glycosylation in cancer diagnostics, treatment, and multidrug resistance. We envision a promising future for the clinical applications of protein glycosylation.

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Role of O-GlcNAcylation on cancer stem cells: Connecting nutrient sensing to cell plasticity

Cited by 5 publications

References 189 publications

Can O-GIcNAc Transferase (OGT) Complex Be Used as a Target for the Treatment of Hematological Malignancies?

Can O-GIcNAc Transferase (OGT) Complex Be Used as a Target for the Treatment of Hematological Malignancies?

O-GlcNAcylation of YTHDF2 antagonizes ERK-dependent phosphorylation and inhibits lung carcinoma

Altered glycosylation in cancer: molecular functions and therapeutic potential

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