ArticleLife science alliance2020
Transglutaminase 2 mediates hypoxia-induced selective mRNA translation via polyamination of 4EBPs.
Article in Life science alliance, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- Arginine shapes growth and mTOR pathway gene expression in Japanese quails (Coturnix japonica).Scientific reports · 2025Article
- Identification of transglutaminase 2 mediated polyaminated proteins in a hepatocellular cancer cell line.Computational and structural biotechnology journal · 2025Article
- Mass Spectrometry of Putrescine, Spermidine, and Spermine Covalently Attached toBiochemistry research international · 2024Article
- The long non-coding RNA PVT1 promotes tumorigenesis of cutaneous squamous cell carcinoma via interaction with 4EBP1.Cell death discovery · 2023Article
- Transglutaminase 2 Prevents Premature Senescence and Promotes Osteoblastic Differentiation of Mesenchymal Stem Cells through NRF2 Activation.Stem cells international · 2023Article
- Transglutaminase 2 mediates transcriptional regulation through BAF250a polyamination.Genes & genomics · 2021Article
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Authors and funding
13 authors at 3 institutions in 1 country.
Funding
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Abstract
Hypoxia selectively enhances mRNA translation despite suppressed mammalian target of rapamycin complex 1 activity, contributing to gene expression reprogramming that promotes metastasis and survival of cancer cells. Little is known about how this paradoxical control of translation occurs. Here, we report a new pathway that links hypoxia to selective mRNA translation. Transglutaminase 2 (TG2) is a hypoxia-inducible factor 1-inducible enzyme that alters the activity of substrate proteins by polyamination or crosslinking. Under hypoxic conditions, TG2 polyaminated eukaryotic translation initiation factor 4E (eIF4E)-bound eukaryotic translation initiation factor 4E-binding proteins (4EBPs) at conserved glutamine residues. 4EBP1 polyamination enhances binding affinity for Raptor, thereby increasing phosphorylation of 4EBP1 and cap-dependent translation. Proteomic analyses of newly synthesized proteins in hypoxic cells revealed that TG2 activity preferentially enhanced the translation of a subset of mRNA containing G/C-rich 5'UTRs but not upstream ORF or terminal oligopyrimidine motifs. These results indicate that TG2 is a critical regulator in hypoxia-induced selective mRNA translation and provide a promising molecular target for the treatment of cancers.
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