ArticleNucleic acids research2017
Control of the negative IRES trans-acting factor KHSRP by ubiquitination.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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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
23 citing papers in PubMed, 193 citations in OpenAlex.
- Article
- Exosomal miR-145-5p from BMSCs alleviates AKI-induced renal fibrosis via KLHL12/KHSRP-mediated m6A-dependent repression of FLI-1.Cell biology and toxicology · 2026Article
- The RNA-Binding Protein KSRP Is a Negative Regulator of Innate Immunity.Biomolecules · 2025Review
- Review
- Cullin 3-mediated ubiquitination restricts enterovirus D68 replication and is counteracted by viral protease 3C.Journal of virology · 2025Article
- Expanding the Functions of KHSRP Protein: Insights into DNA G-Quadruplex Binding.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Insight into the Life Cycle of Enterovirus-A71.Viruses · 2025Review
- VP3 protein of Senecavirus A promotes viral IRES-driven translation and attenuates innate immunity by specifically relocalizing hnRNPA2B1.Journal of virology · 2024Article
- Acetylated KHSRP impairs DNA-damage-response-related mRNA decay and facilitates prostate cancer tumorigenesis.Molecular oncology · 2024Article
- Role of protein Post-translational modifications in enterovirus infection.Frontiers in microbiology · 2024Review
- Genomic and Transcriptional Profiles ofInternational journal of molecular sciences · 2023Article
- Tumor suppressor mediated ubiquitylation of hnRNPK is a barrier to oncogenic translation.Nature communications · 2022Article
- The Role of KH-Type Splicing Regulatory Protein (KSRP) for Immune Functions and Tumorigenesis.Cells · 2022Review
- Curcumin assists anti-EV71 activity of IFN-α by inhibiting IFNAR1 reduction in SH-SY5Y cells.Gut pathogens · 2022Article
- Review
- The roles of KLHL family members in human cancers.American journal of cancer research · 2022Review
- Post-translational Control of RNA-Binding Proteins and Disease-Related Dysregulation.Frontiers in molecular biosciences · 2021Review
- E3 Ligase FBXW2 Is a New Therapeutic Target in Obesity and Atherosclerosis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020Article
- Picornaviruses and RNA Metabolism: Local and Global Effects of Infection.Journal of virology · 2019Review
- Widespread Translational Control of Fibrosis in the Human Heart by RNA-Binding Proteins.Circulation · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cells and viruses can utilize internal ribosome entry sites (IRES) to drive translation when cap-dependent translation is inhibited by stress or viral factors. IRES trans-acting factors (ITAFs) are known to participate in such cap-independent translation, but there are gaps in the understanding as to how ITAFs, particularly negative ITAFs, regulate IRES-driven translation. This study found that Lys109, Lys121 and Lys122 represent critical ubiquitination sites for far upstream element-binding protein 2 (KHSRP, also known as KH-type splicing regulatory protein or FBP2), a negative ITAF. Mutations at these sites subsequently reduced KHSRP ubiquitination and abolished its inhibitory effect on IRES-driven translation. We further found that interaction between the Kelch domain of Kelch-like protein 12 (KLHL12) and the C-terminal domain of KHSRP contributed to KHSRP ubiquitination, leading to downregulation of enterovirus IRES-mediated translation in infected cells and increased competition against other positive ITAFs. Together, these results show that ubiquitination can exert control over IRES-driven translation via modification of ITAFs, and to the best of our knowledge, this is the first description of such a regulatory mechanism for IRES-dependent translation.
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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.