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.

scholarly journals Bovine prion protein as a modulator of protein kinase CK2

2000 ◽  
Vol 352 (1) ◽  
pp. 191-196 ◽  
Author(s):  
Flavio MEGGIO ◽  
Alessandro NEGRO ◽  
Stefania SARNO ◽  
Maria RUZZENE ◽  
Alessandro BERTOLI ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Prion Protein ◽  
Protein Kinase Ck2 ◽  
Truncated Form ◽  
Full Size ◽  
Kinase Ck2 ◽  
The Brain ◽  
Α Subunits ◽  
Far Western Blot ◽  
Stimulation Of

On the basis of far-Western blot and plasmon resonance (BIAcore) experiments, we show here that recombinant bovine prion protein (bPrP) (25–242) strongly interacts with the catalytic α/α´ subunits of protein kinase CK2 (also termed ‘casein kinase 2’). This association leads to increased phosphotransferase activity of CK2α, tested on calmodulin or specific peptides as substrate. We also show that bPrP counteracts the inhibition of calmodulin phosphorylation promoted by the regulatory β subunits of CK2. A truncated form of bPrP encompassing the C-terminal domain (residues 105–242) interacts with CK2 but does not affect its catalytic activity. The opposite is found with the N-terminal fragment of bPrP (residues 25–116), although the stimulation of catalysis is less efficient than with full-size bPrP. These results disclose the potential of the PrP to modulate the activity of CK2, a pleiotropic protein kinase that is particularly abundant in the brain.

The crystal structure of the complex of Zea maysα subunit with a fragment of human β subunit provides the clue to the architecture of protein kinase CK2 holoenzyme

2000 ◽  
Vol 267 (16) ◽  
pp. 5184-5190 ◽  
Author(s):  
Roberto Battistutta ◽  
Stefania Sarno ◽  
Erika De Moliner ◽  
Oriano Marin ◽  
Olaf-G. Issinger ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Β Subunit ◽  
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 The regulatory β-subunit of protein kinase CK2 regulates cell-cycle progression at the onset of mitosis

Oncogene ◽  
2008 ◽  
Vol 27 (37) ◽  
pp. 4986-4997 ◽  
Author(s):  
C W Yde ◽  
B B Olsen ◽  
D Meek ◽  
N Watanabe ◽  
B Guerra
Keyword(s):  
Cell Cycle ◽  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Cell Cycle Progression ◽  
Β Subunit ◽  
Cycle Progression ◽  
Kinase Ck2

Overexpression of Nuclear Protein Kinase CK2 β Subunit and Prognosis in Human Gastric Carcinoma

2010 ◽  
Vol 17 (6) ◽  
pp. 1695-1702 ◽  
Author(s):  
Kai-Yuan Lin ◽  
Chia-Lang Fang ◽  
Yi Chen ◽  
Chien-Feng Li ◽  
Sheng-Hsuan Chen ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Gastric Carcinoma ◽  
Protein Kinase Ck2 ◽  
Nuclear Protein ◽  
Β Subunit ◽  
Human Gastric Carcinoma ◽  
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

scholarly journals Protein Kinase CK2 Subunits Differentially Perturb the Adhesion and Migration of GN11 Cells: A Model of Immature Migrating Neurons

2019 ◽  
Vol 20 (23) ◽  
pp. 5951 ◽  
Author(s):  
Antonella Lettieri ◽  
Christian Borgo ◽  
Luca Zanieri ◽  
Claudio D’Amore ◽  
Roberto Oleari ◽  
...  
Keyword(s):  
Cell Migration ◽  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Primary Role ◽  
Functional Requirements ◽  
Adhesion Properties ◽  
And Migration ◽  
The Individual ◽  
Kinase Ck2

Protein kinase CK2 (CK2) is a highly conserved and ubiquitous kinase is involved in crucial biological processes, including proliferation, migration, and differentiation. CK2 holoenzyme is a tetramer composed by two catalytically active (α/α’) and two regulatory (β) subunits and exerts its function on a broad range of targets. In the brain, it regulates different steps of neurodevelopment, such as neural differentiation, neuritogenesis, and synaptic plasticity. Interestingly, CK2 mutations have been recently linked to neurodevelopmental disorders; however, the functional requirements of the individual CK2 subunits in neurodevelopment have not been yet investigated. Here, we disclose the role of CK2 on the migration and adhesion properties of GN11 cells, an established model of mouse immortalized neurons, by different in vitro experimental approaches. Specifically, the cellular requirement of this kinase has been assessed pharmacologically and genetically by exploiting CK2 inhibitors and by generating subunit-specific CK2 knockout GN11 cells (with a CRISPR/Cas9-based approach). We show that CK2α’ subunit has a primary role in increasing cell adhesion and reducing migration properties of GN11 cells by activating the Akt-GSK3β axis, whereas CK2α subunit is dispensable. Further, the knockout of the CK2β regulatory subunits counteracts cell migration, inducing dramatic alterations in the cytoskeleton not observed in CK2α’ knockout cells. Collectively taken, our data support the view that the individual subunits of CK2 play different roles in cell migration and adhesion properties of GN11 cells, supporting independent roles of the different subunits in these processes.

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