ArticleMolecular and cellular biochemistry2005
Autophosphorylation at the regulatory beta subunit reflects the supramolecular organization of protein kinase CK2.
Article in Molecular and cellular biochemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Review
- CK2β Regulates Hematopoietic Stem Cell Biology and Erythropoiesis.HemaSphere · 2023Article
- Protein kinase CK2 - diverse roles in cancer cell biology and therapeutic promise.Molecular and cellular biochemistry · 2023Review
- Analyzing the interactome of human CK2β in prostate carcinoma cells reveals HSP70-1 and Rho guanin nucleotide exchange factor 12 as novel interaction partners.FASEB bioAdvances · 2023Article
- CIGB-300 anticancer peptide regulates the protein kinase CK2-dependent phosphoproteome.Molecular and cellular biochemistry · 2020Article
- Discovery of holoenzyme-disrupting chemicals as substrate-selective CK2 inhibitors.Scientific reports · 2019Article
- A π-Halogen Bond of Dibenzofuranones with the Gatekeeper Phe113 in Human Protein Kinase CK2 Leads to Potent Tight Binding Inhibitors.Pharmaceuticals (Basel, Switzerland) · 2018Article
- The Development of CK2 Inhibitors: From Traditional Pharmacology to in Silico Rational Drug Design.Pharmaceuticals (Basel, Switzerland) · 2017Review
- Mass Spectrometry Reveals Protein Kinase CK2 High-Order Oligomerization via the Circular and Linear Assembly.ACS chemical biology · 2016Article
- Evidence for aggregation of protein kinase CK2 in the cell: a novel strategy for studying CK2 holoenzyme interaction by BRET(2).Molecular and cellular biochemistry · 2014Article
- Identification of the phosphorylated residues in TveIF5A by mass spectrometry.Genomics, proteomics & bioinformatics · 2013Article
- Casein kinase 2 is essential for mitophagy.EMBO reports · 2013Article
- Phosphorylation of maize eukaryotic translation initiation factor 5A (eIF5A) by casein kinase 2: identification of phosphorylated residue and influence on intracellular localization of eIF5A.The Journal of biological chemistry · 2010Article
- Differential phosphorylation of plant translation initiation factors by Arabidopsis thaliana CK2 holoenzymes.The Journal of biological chemistry · 2009Article
- A role for casein kinase 2 in the mechanism underlying circadian temperature compensation.Cell · 2009Article
- Casein kinase 2 regulates the active uptake of the organic osmolyte taurine in NIH3T3 mouse fibroblasts.Pflugers Archiv : European journal of physiology · 2008Article
- CK2alpha/CK1alpha chimeras are sensitive to regulation by the CK2beta subunit.Molecular and cellular biochemistry · 2008Article
- Biochemical characterization of CK2alpha and alpha' paralogues and their derived holoenzymes: evidence for the existence of a heterotrimeric CK2alpha'-holoenzyme forming trimeric complexes.Molecular and cellular biochemistry · 2008Article
- Modulation of protein kinase CK2 activity by fragments of CFTR encompassing F508 may reflect functional links with cystic fibrosis pathogenesis.Biochemistry · 2008Article
- Analysis of protein kinase autophosphorylation using expressed protein ligation and computational modeling.Journal of the American Chemical Society · 2008Article
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6 authors.
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Abstract
Among the features of protein kinase CK2, autophosphorylation at its beta-subunit(s) upon incubation with ATP/Mg++ was early detected as a rapid and stoichiometric event occurring through an intramolecular mechanism as judged from kinetic analyses. The autophosphorylation site was mapped to Ser2 and, to a lesser extent, Ser3 both fulfilling the CK2 consensus sequence (MSSSEEV). The crystal structure of the heterotetrameric holoenzyme, however, is not compatible with an intramolecular autophosphorylation of the N-terminal stretch of either of the two beta subunits. Here we show that efficient "intramolecular" autophosphorylation of the beta subunit is crucially dependent on the formation of oligomers composed by several holoenzyme heterotetrameric protomers. Increasing ionic strength of the incubation medium promoting dissociation of the supramolecular oligomers abrogates beta subunit autophosphorylation, although CK2 catalytic activity, as judged from the phosphorylation of exogenous substrates, is still quite evident. These findings, in conjunction with graphic modelization, support the view that CK2 autophosphorylation at its beta subunits takes place through an "intraoligomeric" mechanism where the beta subunits of a protomer are phosphorylated by the catalytic subunits of another adjacent protomer. It appears therefore that in vivo beta autophosphorylation is symptomatic of supramolecular CK2 oligomers.
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