ArticleRNA biology
Interplay between Y-box-binding protein 1 (YB-1) and poly(A) binding protein (PABP) in specific regulation of YB-1 mRNA translation.
Article in RNA biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 45 citations in OpenAlex.
- YBX1: A Multifunctional Protein in Senescence and Immune Regulation.Current issues in molecular biology · 2024Review
- Interfering with Rac1-activation during neonatal monocyte-macrophage differentiation influences the inflammatory responses of M1 macrophages.Cell death & disease · 2023Article
- Dual Leucine Zipper Kinase Regulates Dscam Expression through a Noncanonical Function of the Cytoplasmic Poly(A)-Binding Protein.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022Article
- Towards the mechanism(s) of YB-3 synthesis regulation by YB-1.RNA biology · 2021Article
- Y-Box Binding Proteins in mRNP Assembly, Translation, and Stability Control.Biomolecules · 2020Review
- YB-3 substitutes YB-1 in global mRNA binding.RNA biology · 2020Article
- The RNA-binding ubiquitin ligase MKRN1 functions in ribosome-associated quality control of poly(A) translation.Genome biology · 2019Article
- Integrative transcriptomic analysis suggests new autoregulatory splicing events coupled with nonsense-mediated mRNA decay.Nucleic acids research · 2019Article
- Expression and network analysis of YBX1 interactors for identification of new drug targets in lung adenocarcinoma.Journal of genomics · 2018Article
- Identification and dynamic changes of RNAs isolated from RALY-containing ribonucleoprotein complexes.Nucleic acids research · 2017Article
- Handshakes and Fights: The Regulatory Interplay of RNA-Binding Proteins.Frontiers in molecular biosciences · 2017Review
- Rice MEL2, the RNA recognition motif (RRM) protein, binds in vitro to meiosis-expressed genes containing U-rich RNA consensus sequences in the 3'-UTR.Plant molecular biology · 2015Article
- AUF-1 and YB-1 independently regulate β-globin mRNA in developing erythroid cells through interactions with poly(A)-binding protein.Mechanisms of development · 2015Article
- YB-1 expression promotes epithelial-to-mesenchymal transition in prostate cancer that is inhibited by a small molecule fisetin.Oncotarget · 2014Article
- The role of cold shock domain proteins in inflammatory diseases.Journal of molecular medicine (Berlin, Germany) · 2014Review
- Alternative forms of Y-box binding protein 1 and YB-1 mRNA.PloS one · 2014Article
- Experimental characterization of the human non-sequence-specific nucleic acid interactome.Genome biology · 2013Article
- YB-1 synthesis is regulated by mTOR signaling pathway.PloS one · 2012Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
YB-1 is a DNA- and RNA-binding protein that regulates expression of many important genes. Its deficiency or excess may pose threats, including malignant cellular transformation and metastasis, which explains the necessity of strict control over its amount at every level. As we showed previously, the 3' untranslated region (UTR) of YB-1 mRNA contains a regulatory element specifically binding to YB-1 and PABP (PABPC1). Also, we showed that YB-1 selectively inhibits YB-1 mRNA translation, while PABP stimulates it in a poly(A) tail-independent manner. It was suggested that regulation of YB-1 mRNA translation involves competition between PABP and YB-1 for binding to the regulatory element. Here we offer cogent evidence for this model and add novel details to the mechanism of regulation of YB-1 synthesis. In experiments on regulatory element deletion we showed that it is this element that is responsible for a specific effect of YB-1 and PABP on YB-1 mRNA translation. Mutations eliminating only specific YB-1 affinity for this element suppressed the inhibitory effect of YB-1 and concurrently dramatically decreased the PABP stimulating effect. Mutations reducing only specific PABP affinity for this element, as well as spatial separation of the YB-1- and PABP binding sites, did not affect the YB-1 inhibitory action but completely abolished the positive PABP effect. Together, these results unambiguously prove direct inhibitory action of YB-1 on its mRNA translation, while the positive effect of PABP is realized through displacing YB-1 from the regulatory element.
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