ArticleThe Biochemical journal2012
TGF-β sensitivity is determined by N-linked glycosylation of the type II TGF-β receptor.
Article in The Biochemical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 130 citations in OpenAlex.
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- Bioinformatics Identification and Molecular Docking Validation of Post-Translational Modification-Related Hub Genes as Diagnostic Biomarkers and Therapeutic Targets in Myocardial Fibrosis.International journal of molecular sciences · 2026Article
- Loss of ALK4 promotes cancer progression through regulating TGF-β receptor N-glycosylation.Nature communications · 2025Article
- B4GALT1-dependent galectin-8 binding with TGF-β receptor suppresses colorectal cancer progression and metastasis.Cell death & disease · 2024Article
- Glycosylation: mechanisms, biological functions and clinical implications.Signal transduction and targeted therapy · 2024Review
- Fluorescent Chiral Quantum Dots to Unveil Origin-Dependent Exosome Uptake and Cargo Release.ACS applied bio materials · 2024Article
- The role ofActa pharmaceutica Sinica. B · 2024Review
- Different glycosylation profiles of cystatin F alter the cytotoxic potential of natural killer cells.Cellular and molecular life sciences : CMLS · 2023Article
- N-linked glycosylation is essential for anti-tumor activities of KIAA1324 in gastric cancer.Cell death & disease · 2023Article
- ST6GALNAC4 promotes hepatocellular carcinogenesis by inducing abnormal glycosylation.Journal of translational medicine · 2023Article
- Transforming growth factor-β1 and SMAD signalling pathway in the small airways of smokers and patients with COPD: potential role in driving fibrotic type-2 epithelial mesenchymal transition.Frontiers in immunology · 2023Article
- Article
- The activation of PPARγ enhances Treg responses through up-regulating CD36/CPT1-mediated fatty acid oxidation and subsequent N-glycan branching of TβRII/IL-2Rα.Cell communication and signaling : CCS · 2022Article
- Molecular Mechanisms of AMH Signaling.Frontiers in endocrinology · 2022Review
- Ionising Radiation Promotes Invasive Potential of Breast Cancer Cells: The Role of Exosomes in the Process.International journal of molecular sciences · 2021Article
- Canonical TGFβ Signaling and Its Contribution to Endometrial Cancer Development and Progression-Underestimated Target of Anticancer Strategies.Journal of clinical medicine · 2021Review
- Role of Glycans on Key Cell Surface Receptors That Regulate Cell Proliferation and Cell Death.Cells · 2021Review
- Glycosylation of Immune Receptors in Cancer.Cells · 2021Review
- ALG3 contributes to stemness and radioresistance through regulating glycosylation of TGF-β receptor II in breast cancer.Journal of experimental & clinical cancer research : CR · 2021Article
- Role of glycosylation in TGF-β signaling and epithelial-to-mesenchymal transition in cancer.Protein & cell · 2021Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N-linked glycosylation is a critical determinant of protein structure and function, regulating processes such as protein folding, stability and localization, ligand-receptor binding and intracellular signalling. TβRII [type II TGF-β (transforming growth factor β) receptor] plays a crucial role in the TGF-β signalling pathway. Although N-linked glycosylation of TβRII was first demonstrated over a decade ago, it was unclear how this modification influenced TβRII biology. In the present study, we show that inhibiting the N-linked glycosylation process successfully hinders binding of TGF-β1 to TβRII and subsequently renders cells resistant to TGF-β signalling. The lung cancer cell line A549, the gastric carcinoma cell line MKN1 and the immortal cell line HEK (human embryonic kidney)-293 exhibit reduced TGF-β signalling when either treated with two inhibitors, including tunicamycin (a potent N-linked glycosylation inhibitor) and kifunensine [an inhibitor of ER (endoplasmic reticulum) and Golgi mannosidase I family members], or introduced with a non-glycosylated mutant version of TβRII. We demonstrate that defective N-linked glycosylation prevents TβRII proteins from being transported to the cell surface. Moreover, we clearly show that not only the complex type, but also a high-mannose type, of TβRII can be localized on the cell surface. Collectively, these findings demonstrate that N-linked glycosylation is essentially required for the successful cell surface transportation of TβRII, suggesting a novel mechanism by which the TGF-β sensitivity can be regulated by N-linked glycosylation levels of TβRII.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.