ArticleProceedings of the National Academy of Sciences of the United States of America2013
Structural and functional insights into the regulation mechanism of CK2 by IP6 and the intrinsically disordered protein Nopp140.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed, 49 citations in OpenAlex.
- Protein pyrophosphorylation by inositol pyrophosphates - detection, function, and regulation.FEBS letters · 2026Review
- Identification of the regulatory elements and protein substrates of lysine acetoacetylation.eLife · 2026Article
- Identification of the Regulatory Elements and Protein Substrates of Lysine Acetoacetylation.bioRxiv : the preprint server for biology · 2025Article
- Article
- SPOP/NOLC1/B4GALT1 signaling axis enhances paclitaxel resistance in endometrial cancer by inducing O-dysglycosylation.Oncogene · 2025Article
- Pools of Independently Cycling Inositol Phosphates Revealed by Pulse Labeling withJournal of the American Chemical Society · 2025Article
- Interaction with IP6K1 supports pyrophosphorylation of substrate proteins by the inositol pyrophosphate 5-InsP7.Bioscience reports · 2024Article
- Multiple inositol phosphate species enhance stability of active mTOR.bioRxiv : the preprint server for biology · 2024Article
- Roles of NOLC1 in cancers and viral infection.Journal of cancer research and clinical oncology · 2023Review
- Phosphoproteomics revealed cellular signals immediately responding to disruption of cancer amino acid homeostasis induced by inhibition of L-type amino acid transporter 1.Cancer & metabolism · 2022Article
- The Role of Protein Kinase CK2 in Development and Disease Progression: A Critical Review.Journal of developmental biology · 2022Review
- Placental Mammals Acquired Functional Sequences in NRK for Regulating the CK2-PTEN-AKT Pathway and Placental Cell Proliferation.Molecular biology and evolution · 2022Article
- Signalling Properties of Inositol Polyphosphates.Molecules (Basel, Switzerland) · 2020Review
- Proposed Allosteric Inhibitors Bind to the ATP Site of CK2α.Journal of medicinal chemistry · 2020Article
- Article
- AThe Journal of biological chemistry · 2020Article
- Structural analyses of inositol phosphate second messengers bound to signaling effector proteins.Advances in biological regulation · 2020Review
- Identity and functions of inorganic and inositol polyphosphates in plants.The New phytologist · 2020Review
- Lamin A buffers CK2 kinase activity to modulate aging in a progeria mouse model.Science advances · 2019Article
- 2-Aminothiazole Derivatives as Selective Allosteric Modulators of the Protein Kinase CK2. 1. Identification of an Allosteric Binding Site.Journal of medicinal chemistry · 2019Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein kinase CK2 is a ubiquitous kinase that can phosphorylate hundreds of cellular proteins and plays important roles in cell growth and development. Deregulation of CK2 is related to a variety of human cancers, and CK2 is regarded as a suppressor of apoptosis; therefore, it is a target of anticancer therapy. Nucleolar phosphoprotein 140 (Nopp140), which is an intrinsically disordered protein, interacts with CK2 and inhibits the latter's catalytic activity in vitro. Interestingly, the catalytic activity of CK2 is recovered in the presence of d-myo-inositol 1,2,3,4,5,6-hexakisphosphate (IP6). IP6 is widely distributed in animal cells, but the molecular mechanisms that govern its cellular functions in animal cells have not been completely elucidated. In this study, the crystal structure of CK2 in complex with IP6 showed that the lysine-rich cluster of CK2 plays an important role in binding to IP6. The biochemical experiments revealed that a Nopp140 fragment (residues 568-596) and IP6 competitively bind to the catalytic subunit of CK2 (CK2α), and phospho-Ser574 of Nopp140 significantly enhances its interaction with CK2α. Substitutions of K74E, K76E, and K77E in CK2α significantly reduced the interactions of CK2α with both IP6 and the Nopp140-derived peptide. Our study gives an insight into the regulation of CK2. In particular, our work suggests that CK2 activity is inhibited by Nopp140 and reactivated by IP6 by competitive binding at the substrate recognition site of CK2.
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