ArticleNucleic acids research2006
Post-transcriptional regulation of thioredoxin by the stress inducible heterogenous ribonucleoprotein A18.
Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
55 citing papers in PubMed, 111 citations in OpenAlex.
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- Glucose-6-Phosphate Dehydrogenase, Redox Homeostasis and Embryogenesis.International journal of molecular sciences · 2022Review
- Downregulation of CIRP Prone Cells to Oxidative Injury via Regulating Nrf2 Signaling Pathway.BioMed research international · 2022Article
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- Absence of Cold-Inducible RNA-Binding Protein (CIRP) Promotes Angiogenesis and Regeneration of Ischemic Tissue by Inducing M2-Like Macrophage Polarization.Biomedicines · 2021Article
- Small molecules inhibitors of the heterogeneous ribonuclear protein A18 (hnRNP A18): a regulator of protein translation and an immune checkpoint.Nucleic acids research · 2021Article
- Cold-inducible RNA binding protein promotes breast cancer cell malignancy by regulating Cystatin C levels.RNA (New York, N.Y.) · 2021Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Thioredoxin (TRX) is a key protein of the cellular redox metabolism, which expression is increased in several tumors especially gastric tumors. Even though ultraviolet (UV) and hypoxia specifically induce TRX, the mechanisms that lead to increased TRX levels are still ill defined. Here, we show that the heterogenous ribonucleoprotein A18 (hnRNP A18) RNA Binding Domain (RBD) and the arginine, glycine (RGG) rich domain can bind TRX 3'-untranslated region (3'-UTR) independently but both domains are required for maximal binding. Immunoprecipitation (IP) of hnRNP A18-mRNAs complexes and co-localization of hnRNP A18 and TRX transcripts on ribosomal fractions confirm the interaction of hnRNP A18 with TRX transcripts in cells. Moreover, down regulation of hnRNP A18 correlates with a significant reduction of TRX protein levels. In addition, hnRNP A18 increases TRX translation and interacts with the eukaryotic Initiation Factor 4G (eIF4G), a component of the general translational machinery. Furthermore, hnRNP A18 phosphorylation by the hypoxia inducible GSK3beta increases hnRNP A18 RNA binding activity in vitro and in RKO cells in response to UV radiation. These data support a regulatory role for hnRNP A18 in TRX post-transcriptional expression possibly through a kissing loop model bridging TRX 3'- and 5'-UTRs through eIF4G.
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Registered trials
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