ArticleThe international journal of biochemistry & cell biology2011
Far upstream element binding protein 1 activates translation of p27Kip1 mRNA through its internal ribosomal entry site.
Article in The international journal of biochemistry & cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 37 citations in OpenAlex.
- c-Jun in neurodegeneration: A key transcriptional regulator with therapeutic implications.Molecular therapy. Nucleic acids · 2026Review
- IRES-Mediated Translation: Expanding the Toolkits of RNA Therapy.International journal of molecular sciences · 2025Review
- A dual effect of FUBP1 onRNA (New York, N.Y.) · 2025Article
- The role of fructose-1,6-bisphosphatase 1 on regulating the cancer progression and drug resistance.Discover oncology · 2025Review
- FUBP1 in human cancer: Characteristics, functions, and potential applications.Translational oncology · 2024Review
- KHSRP loss increases neuronal growth and synaptic transmission and alters memory consolidation through RNA stabilization.Communications biology · 2022Article
- Using protein microarray to identify and evaluate autoantibodies to tumor-associated antigens in ovarian cancer.Cancer science · 2021Article
- The master regulator FUBP1: its emerging role in normal cell function and malignant development.Cellular and molecular life sciences : CMLS · 2019Review
- Article
- Interplay between transcription regulators RUNX1 and FUBP1 activates an enhancer of the oncogene c-KIT and amplifies cell proliferation.Nucleic acids research · 2018Article
- Cold-inducible RNA-binding protein (CIRP) induces translation of the cell-cycle inhibitor p27Kip1.Nucleic acids research · 2018Article
- More than just scanning: the importance of cap-independent mRNA translation initiation for cellular stress response and cancer.Cellular and molecular life sciences : CMLS · 2017Review
- Article
- Additive Promotion of Viral Internal Ribosome Entry Site-Mediated Translation by Far Upstream Element-Binding Protein 1 and an Enterovirus 71-Induced Cleavage Product.PLoS pathogens · 2016Article
- IRES inhibition induces terminal differentiation and synchronized death in triple-negative breast cancer and glioblastoma cells.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016Article
- Far upstream element-binding protein 1 (FUBP1) is a potential c-Myc regulator in esophageal squamous cell carcinoma (ESCC) and its expression promotes ESCC progression.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016Article
- Far upstream element-binding protein 1 is a prognostic biomarker and promotes nasopharyngeal carcinoma progression.Cell death & disease · 2015Article
- Small molecule inhibitors of IRES-mediated translation.Cancer biology & therapy · 2015Article
- The splicing factor FUBP1 is required for the efficient splicing of oncogene MDM2 pre-mRNA.The Journal of biological chemistry · 2014Article
- p27 is regulated independently of Skp2 in the absence of Cdk2.Biochimica et biophysica acta · 2014Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
The cyclin dependent kinase inhibitor p27 plays an important role in controlling the eukaryotic cell cycle by regulating progression through G1 and entry into S phase. It is often elevated during differentiation and under conditions of cellular stress. In contrast, it is commonly downregulated in cancer cells and its levels are generally inversely correlated with favorable prognosis. The cellular levels of p27 are regulated, in part, by translational control mechanisms. The 5'-untranslated region (5'-UTR) of the p27 mRNA harbors an internal ribosome entry site (IRES) which may facilitate synthesis of p27 in certain conditions. In this study, Far Upstream Element (FUSE) Binding Protein 1 (FBP1) was shown to directly bind to the human p27 5'-UTR and to promote IRES activity. An eight-nucleotide element downstream of a U-rich region within the 5'-UTR was important for FBP1 binding and p27 IRES activity. Overexpression of FBP1 enhanced endogenous p27 levels and stimulated translation initiation. In contrast, repression of FBP1 by siRNA transfection downregulated endogenous p27 protein levels. Using rabbit reticulocyte lysates, FBP1 stimulated p27 mRNA translation in vitro. The central domain of FBP1, containing four K homology motifs, was required for p27 5'-UTR RNA binding and the N terminal domain was important for translational activation. These findings indicate that FBP1 is a novel activator of p27 translation upon binding to the 5'-UTR.
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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.