Specific localization of the catalytic subunits of protein kinase CK2 at the centrosomes

2002 ◽  
Vol 59 (12) ◽  
pp. 2155-2164 ◽  
Author(s):  
M. Faust ◽  
J. Günther ◽  
E. Morgenstern ◽  
M. Montenarh ◽  
C. Götz
Keyword(s):  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Catalytic Subunits ◽  
Specific Localization ◽  
Kinase Ck2

Phosphorylation of thymidylate synthase from various sources by human protein kinase CK2 and its catalytic subunits

2010 ◽  
Vol 38 (3) ◽  
pp. 124-131 ◽  
Author(s):  
Tomasz Frączyk ◽  
Konrad Kubiński ◽  
Maciej Masłyk ◽  
Joanna Cieśla ◽  
Ulf Hellman ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Thymidylate Synthase ◽  
Protein Kinase Ck2 ◽  
Human Protein ◽  
Catalytic Subunits ◽  
Human Protein Kinase ◽  
Kinase Ck2

scholarly journals Specific binding of protein kinase CK2 catalytic subunits to tubulin

FEBS Letters ◽  
1999 ◽  
Vol 462 (1-2) ◽  
pp. 51-56 ◽  
Author(s):  
Michael Faust ◽  
Norbert Schuster ◽  
Mathias Montenarh
Keyword(s):  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Specific Binding ◽  
Catalytic Subunits ◽  
Kinase Ck2

Protein kinase CK2 from two higher eukaryotes of economical importance, the mussel Mytilus galloprovincialis and the medfly Ceratitis capitata

2012 ◽  
Vol 7 (2) ◽  
pp. 185-191
Author(s):  
Sophia Kouyanou-Koutsoukou ◽  
Andrea Baier ◽  
Regina-Maria Kolaitis ◽  
Ryszard Szyszka
Keyword(s):  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Mytilus Galloprovincialis ◽  
Ceratitis Capitata ◽  
Marine Pollution ◽  
Cell Cycle Control ◽  
Control Of Gene Expression ◽  
Catalytic Subunits ◽  
Wide Range ◽  
Kinase Ck2

AbstractProtein kinase CK2 is a highly conserved Ser/Thr protein kinase involved in cell cycle control, transcription, signal transduction and cell proliferation. It is upregulated in several diseases and by oxidative stress. CK2 is generally composed of two catalytic subunits and two regulatory subunits and utilizes either ATP or GTP as a phosphate donor. CK2 was isolated from the sea mussel Mytilus galloprovincialis, a biomarker of marine pollution, and the Mediterranean fly Ceratitis capitata, an insect capable of wreaking extensive damage to a wide range of fruit crops with great economical importance. The catalytic CK2α and regulatory CK2β subunits of M. galloprovincialis and C. capitata show similar properties. The mussel and fly catalytic subunits and holoenzymes were capable of phosphorylating the recombinant ribosomal stalk P1 protein, implying functional conservation. They also demonstrate the characteristics of a typical CK2: use of ATP and GTP as phosphate donors, inhibition by known modulators of CK2 activity (like benzotriazole derivatives and heparin), and stimulation by polycations. Both organisms seem to be ideal models for the analysis of CK2 in the control of gene expression in response to cellular stress.

scholarly journals Down-regulation of CK2α correlates with decreased expression levels of DNA replication minichromosome maintenance protein complex (MCM) genes

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Susanne Schaefer ◽  
Thomas K. Doktor ◽  
Sabrina B. Frederiksen ◽  
Kathleen Chea ◽  
Mirka Hlavacova ◽  
...  
Keyword(s):  
Gene Expression ◽  
Cell Cycle ◽  
Cell Proliferation ◽  
Dna Replication ◽  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Minichromosome Maintenance ◽  
Catalytic Subunits ◽  
Expression Levels ◽  
Kinase Ck2

Abstract Protein kinase CK2 is a serine/threonine kinase composed of two catalytic subunits (CK2α and/or CK2α’) and two regulatory subunits (CK2β). It is implicated in every stage of the cell cycle and in the regulation of various intracellular pathways associated with health and disease states. The catalytic subunits have similar biochemical activity, however, their functions may differ significantly in cells and in vivo. In this regard, homozygous deletion of CK2α leads to embryonic lethality in mid-gestation potentially due to severely impaired cell proliferation. To determine the CK2α-dependent molecular mechanisms that control cell proliferation, we established a myoblast-derived cell line with inducible silencing of CK2α and carried out a comprehensive RNA-Seq analysis of gene expression. We report evidence that CK2α depletion causes delayed cell cycle progression through the S-phase and defective response to replication stress. Differential gene expression analysis revealed that the down-regulated genes were enriched in pathways implicated in cell cycle regulation, DNA replication and DNA damage repair. Interestingly, the genes coding for the minichromosome maintenance proteins (MCMs), which constitute the core of the replication origin recognition complex, were among the most significantly down-regulated genes. These findings were validated in cells and whole mouse embryos. Taken together, our study provides new evidence for a critical role of protein kinase CK2 in controlling DNA replication initiation and the expression levels of replicative DNA helicases, which ensure maintenance of proliferative potential and genome integrity in eukaryotic cells.

Autocatalytic tyrosine-phosphorylation of protein kinase CK2 α and α′ subunits: implication of Tyr182

2001 ◽  
Vol 357 (2) ◽  
pp. 563-567 ◽  
Author(s):  
Arianna DONELLA-DEANA ◽  
Luca CESARO ◽  
Stefania SARNO ◽  
Anna Maria BRUNATI ◽  
Maria RUZZENE ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Activation Loop ◽  
Β Subunit ◽  
Catalytic Subunits ◽  
The Individual ◽  
Kinase Ck2 ◽  
Tyrosine Autophosphorylation ◽  
Α Subunits

CK2 is a pleiotropic and constitutively active serine/threonine protein kinase composed of two catalytic (α and/or α′) and two regulatory β-subunits, whose mechanism of modulation is still obscure. Here we show that CK2 α/α′ subunits undergo intermolecular (trans) tyrosine-autophosphorylation, which is dependent on intrinsic catalytic activity and is suppressed by the individual mutation of Tyr182, a crucial residue of the activation loop, to phenylalanine. At variance with serine-autophosphorylation, tyrosine-autophosphorylation of CK2α is reversed by ADP and GDP and is counteracted by the β-subunit and by a peptide reproducing the activation loop of CK2α/α′ (amino acids 175–201). These results disclose new perspectives about the mode of regulation of CK2 catalytic subunits.

Assembly of protein kinase CK2: investigation of complex formation between catalytic and regulatory subunits using a zinc-finger-deficient mutant of CK2β

2001 ◽  
Vol 358 (1) ◽  
pp. 87-94 ◽  
Author(s):  
David A. CANTON ◽  
Cunjie ZHANG ◽  
David W. LITCHFIELD
Keyword(s):  
Protein Kinase ◽  
Zinc Finger ◽  
Protein Kinase Ck2 ◽  
Deficient Mutant ◽  
Binding Assays ◽  
Catalytic Subunits ◽  
Regulatory Subunits ◽  
Regulatory Ck2β Subunit ◽  
Kinase Ck2

Protein kinase CK2 is a tetrameric enzyme comprised of two regulatory subunits (CK2β) and two catalytic subunits (CK2α and/or CK2α′). The crystal structure of dimeric CK2β demonstrated that a zinc finger mediates CK2β dimerization, therefore we constructed a mutant in which cysteine residues 109 and 114 were mutated to serine. Our objectives were to examine the effects of disrupting the zinc finger of the regulatory CK2β subunit on CK2 tetramer assembly. Examination of this zinc-finger-deficient mutant of CK2β using a yeast two-hybrid assay demonstrates that the mutant fails to form CK2β homodimers. In order to extend these studies, we co-transfected COS-7 cells with epitope-tagged constructs and performed co-immunoprecipitation assays. The results from these studies demonstrate that the mutant fails to form CK2β homodimers and fails to interact with catalytic CK2 subunits. Furthermore, we demonstrate that the mutant CK2β is not appreciably phosphorylated in cells. Using in vitro binding assays, we demonstrated that the mutant CK2β protein fails to interact with glutathione S-transferase–CK2α′. Finally, we demonstrate that the mutant is translated at an equivalent rate to wild-type CK2β, but is degraded much more rapidly. Overall, our results are consistent with the model that β–β dimerization precedes incorporation of catalytic subunits into tetrameric CK2 complexes, and that β–β dimerization is a prerequisite for the stable incorporation of catalytic subunits into CK2 complexes.

Sign in / Sign up

Export Citation Format

Share Document