ArticlePloS one2010
A conserved stem loop motif in the 5'untranslated region regulates transforming growth factor-β(1) translation.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 37 citations in OpenAlex.
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- Cold shock proteins: from cellular mechanisms to pathophysiology and disease.Cell communication and signaling : CCS · 2018Review
- The Protozoan Parasite Toxoplasma gondii Selectively Reprograms the Host Cell Translatome.Infection and immunity · 2018Article
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- Interplay between YB-1 and IL-6 promotes the metastatic phenotype in breast cancer cells.Oncotarget · 2015Article
- Cis-regulatory RNA elements that regulate specialized ribosome activity.RNA biology · 2015Review
- Novel RNA-binding protein P311 binds eukaryotic translation initiation factor 3 subunit b (eIF3b) to promote translation of transforming growth factor β1-3 (TGF-β1-3).The Journal of biological chemistry · 2014Article
- The role of cold shock domain proteins in inflammatory diseases.Journal of molecular medicine (Berlin, Germany) · 2014Review
- YB-1 stabilizes HIV-1 genomic RNA and enhances viral production.Protein & cell · 2013Article
- Global or local? Predicting secondary structure and accessibility in mRNAs.Nucleic acids research · 2012Article
- YB-1, the E2F pathway, and regulation of tumor cell growth.Journal of the National Cancer Institute · 2012Article
- Before It Gets Started: Regulating Translation at the 5' UTR.Comparative and functional genomics · 2012Article
- Post-transcriptional regulation of Transforming Growth Factor Beta-1 by microRNA-744.PloS one · 2011Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transforming growth factor-β(1) (TGF-β(1)) regulates cellular proliferation, differentiation, migration, and survival. The human TGF-β(1) transcript is inherently poorly translated, and translational activation has been documented in relation to several stimuli. In this paper, we have sought to identify in cis regulatory elements within the TGF-β(1) 5'Untranslated Region (5'UTR). In silico analysis predicted formation of stable secondary structure in a G/C-rich element between nucleotides +77 to +106, and demonstrated that this element is highly conserved across species. Circular dichroism spectroscopy confirmed the presence of secondary structure in this region. The proximal 5'UTR was inhibitory to translation in reporter gene experiments, and mutation of the secondary structure motif increased translational efficiency. Translational regulation of TGF-β(1) mRNA is linked to altered binding of YB-1 protein to its 5'UTR. Immunoprecipitation-RT-qPCR demonstrated a high basal association of YB-1 with TGF-β(1) mRNA. However, mutation of the secondary structure motif did not prevent interaction of YB-1 with the 5'UTR, suggesting that YB-1 binds to this region due to its G/C-rich composition, rather than a specific, sequence-dependent, binding site. These data identify a highly conserved element within the TGF-β(1) 5'UTR that forms stable secondary structure, and is responsible for the inherent low translation efficiency of this cytokine.
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