ArticlePloS one2012
Interaction of Rio1 kinase with toyocamycin reveals a conformational switch that controls oligomeric state and catalytic activity.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 37 citations in OpenAlex.
- The ribosomal landscape in influenza A virus infection: from molecular mechanisms to clinical relevance.European respiratory review : an official journal of the European Respiratory Society · 2026Review
- Serine/Threonine Protein Kinases as Attractive Targets for Anti-Cancer Drugs-An Innovative Approach to Ligand Tuning Using Combined Quantum Chemical Calculations, Molecular Docking, Molecular Dynamic Simulations, and Network-like Similarity Graphs.Molecules (Basel, Switzerland) · 2024Article
- Pathways controlling neurotoxicity and proteostasis in mitochondrial complex I deficiency.Human molecular genetics · 2024Article
- The RioK1 network determines p53 activity at multiple levels.Cell death discovery · 2023Article
- The Oncogenic Protein Kinase/ATPase RIOK1 Is Up-Regulated via the c-myc/E2F Transcription Factor Axis in Prostate Cancer.The American journal of pathology · 2023Article
- Riok1, A Novel Potential Target in MSI-High p53 Mutant Colorectal Cancer Cells.Molecules (Basel, Switzerland) · 2023Article
- Concentrative Nucleoside Transporter, CNT, Results in Selective Toxicity of Toyocamycin against Candida albicans.Microbiology spectrum · 2022Article
- Article
- First Evidence of Function forPathogens (Basel, Switzerland) · 2021Article
- Selective regulation in ribosome biogenesis and protein production for efficient viral translation.Archives of microbiology · 2021Review
- Substrate inhibition by the blockage of product release and its control by tunnel engineering.RSC chemical biology · 2021Article
- Chemical genetic approach using β-rubromycin reveals that a RIO kinase-like protein is involved in morphological development in Phytophthora infestans.Scientific reports · 2020Article
- A kinase-dependent checkpoint prevents escape of immature ribosomes into the translating pool.PLoS biology · 2019Article
- In vitro dimerization of human RIO2 kinase.RNA biology · 2019Article
- Conformational Studies of Glucose Transporter 1 (GLUT1) as an Anticancer Drug Target.Molecules (Basel, Switzerland) · 2019Article
- The Rio1 protein kinases/ATPases: conserved regulators of growth, division, and genomic stability.Current genetics · 2019Review
- Integrating Rio1 activities discloses its nutrient-activated network in Saccharomyces cerevisiae.Nucleic acids research · 2018Article
- A novel cell-based screening assay for small-molecule MYB inhibitors identifies podophyllotoxins teniposide and etoposide as inhibitors of MYB activity.Scientific reports · 2018Article
- The Atypical Kinase RIOK1 Promotes Tumor Growth and Invasive Behavior.EBioMedicine · 2017Article
- The Link between Protein Kinase CK2 and Atypical Kinase Rio1.Pharmaceuticals (Basel, Switzerland) · 2017Review
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
Rio1 kinase is an essential ribosome-processing factor required for proper maturation of 40 S ribosomal subunit. Although its structure is known, several questions regarding its functional remain to be addressed. We report that both Archaeoglobus fulgidus and human Rio1 bind more tightly to an adenosine analog, toyocamycin, than to ATP. Toyocamycin has antibiotic, antiviral and cytotoxic properties, and is known to inhibit ribosome biogenesis, specifically the maturation of 40 S. We determined the X-ray crystal structure of toyocamycin bound to Rio1 at 2.0 Å and demonstrated that toyocamycin binds in the ATP binding pocket of the protein. Despite this, measured steady state kinetics were inconsistent with strict competitive inhibition by toyocamycin. In analyzing this interaction, we discovered that Rio1 is capable of accessing multiple distinct oligomeric states and that toyocamycin may inhibit Rio1 by stabilizing a less catalytically active oligomer. We also present evidence of substrate inhibition by high concentrations of ATP for both archaeal and human Rio1. Oligomeric state studies show both proteins access a higher order oligomeric state in the presence of ATP. The study revealed that autophosphorylation by Rio1 reduces oligomer formation and promotes monomerization, resulting in the most active species. Taken together, these results suggest the activity of Rio1 may be modulated by regulating its oligomerization properties in a conserved mechanism, identifies the first ribosome processing target of toyocamycin and presents the first small molecule inhibitor of Rio1 kinase activity.
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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.