ArticleThe Biochemical journal2005
Characterization of a new family of cyclin-dependent kinase activators.
Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
27 citing papers in PubMed, 57 citations in OpenAlex.
- The non-canonical CDK2 activator SPY1 uses separable mechanisms to activate phosphorylated and unphosphorylated CDK2.The Biochemical journal · 2026Article
- CDK6 is activated by the atypical cyclin I to promote E2F-mediated gene expression and cancer cell proliferation.Molecular oncology · 2023Article
- Article
- Genome-Wide Detection of Copy Number Variations and Their Association With Distinct Phenotypes in the World's Sheep.Frontiers in genetics · 2021Article
- A novel function for CDK2 activity at meiotic crossover sites.PLoS biology · 2020Article
- Atypical cyclins: the extended family portrait.Cellular and molecular life sciences : CMLS · 2020Review
- Diverse roles for CDK-associated activity during spermatogenesis.FEBS letters · 2019Review
- Structural basis of divergent cyclin-dependent kinase activation by Spy1/RINGO proteins.The EMBO journal · 2017Article
- Revisiting CDK Inhibitors for Treatment of Glioblastoma Multiforme.Drugs in R&D · 2017Review
- Speedy A-Cdk2 binding mediates initial telomere-nuclear envelope attachment during meiotic prophase I independent of Cdk2 activation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Essential role of the Cdk2 activator RingoA in meiotic telomere tethering to the nuclear envelope.Nature communications · 2016Article
- Spy1 Protein Mediates Phosphorylation and Degradation of SCG10 Protein in Axonal Degeneration.The Journal of biological chemistry · 2015Article
- The atypical cell cycle regulator Spy1 suppresses differentiation of the neuroblastoma stem cell population.Oncoscience · 2014Article
- Cell adhesion to fibronectin down-regulates the expression of Spy1 and contributes to drug resistance in multiple myeloma cells.International journal of hematology · 2013Article
- Role of LM23 in cell proliferation and apoptosis and its expression during the testis development.Asian journal of andrology · 2013Article
- Temporal-spatial expressions of Spy1 in rat sciatic nerve after crush.Cellular and molecular neurobiology · 2013Article
- Evolution of the Cdk-activator Speedy/RINGO in vertebrates.Cellular and molecular life sciences : CMLS · 2012Article
- Spy1 is frequently overexpressed in malignant gliomas and critically regulates the proliferation of glioma cells.Journal of molecular neuroscience : MN · 2012Article
- Translational regulation of the cell cycle: when, where, how and why?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2011Review
- LM23 is a novel member of the Speedy/Ringo family at the crossroads of life and death of spermatogenic cell.Asian journal of andrology · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Progression through the cell cycle is regulated by CDKs (cyclin-dependent kinases), which associate with activating partners, named cyclins, to efficiently phosphorylate substrates. We previously reported the identification of RINGO, a Xenopus protein that can activate CDK1 and CDK2 despite lack of sequence similarity to cyclins, which plays a role in the regulation of the meiotic cell cycle in oocytes. In the present study we report the characterization of four mammalian RINGO proteins, which are 53-68% identical with Xenopus RINGO in a central core of about 75 residues. We show that all RINGO family members can bind to and activate CDK1 and CDK2, albeit with different efficiencies, but they do not bind to CDK4 or CDK6. The core RINGO sequences are critical for CDK activation. We also identified key residues in CDK2 that are required for RINGO binding. All RINGO proteins can also bind the CDK inhibitor p27Kip1, but with an inverse efficiency of their ability to bind to CDK1. Our results identify a new family of mammalian proteins that can activate CDKs and therefore potentially function as cell cycle regulators. The ability of RINGO proteins to activate CDK1 and CDK2 suggest also cyclin-independent roles for these kinases.
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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.