Autophosphorylation at the regulatory beta subunit reflects the supramolecular organization of protein kinase CK2. (Q46840846)

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10 January 2020

title

Autophosphorylation at the regulatory beta subunit reflects the supramolecular organization of protein kinase CK2 (English)

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10 January 2020

1

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10 January 2020

Giorgio Cozza

4

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10 January 2020

Stefania Sarno

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author name string

Giorgia Poletto

3

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10 January 2020

Lorenzo A Pinna

5

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10 January 2020

Flavio Meggio

6

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10 January 2020

publication date

1 June 2005

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Molecular and Cellular Biochemistry

10 January 2020

published in

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10 January 2020

volume

274

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10 January 2020

issue

1-2

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10 January 2020

page(s)

23-29

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https://scigraph.springernature.com/pub.10.1007/s11010-005-3116-y

10 January 2020

exact match

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cites work

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Protein Kinase CK2 Mutants Defective in Substrate Recognition

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Casein kinase 2: an 'eminence grise' in cellular regulation?

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Phosphorylation regulates the stability of the regulatory CK2beta subunit

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ESCHER: a new docking procedure applied to the reconstruction of protein tertiary structure

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Ser2 is the autophosphorylation site in the beta subunit from bicistronically expressed human casein kinase-2 and from native rat liver casein kinase-2 beta

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Protein kinases. 4. Protein kinase CK2: an enzyme with multiple substrates and a puzzling regulation

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Structural basis of regulation and substrate specificity of protein kinase CK2 deduced from the modeling of protein-protein interactions

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A majority of casein kinase II alpha subunit is tightly bound to intranuclear components but not to the beta subunit

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Protein kinase CK2: evidence for a protein kinase CK2beta subunit fraction, devoid of the catalytic CK2alpha subunit, in mouse brain and testicles

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Efficient autophosphorylation and phosphorylation of the beta-subunit by casein kinase-2 require the integrity of an acidic cluster 50 residues downstream from the phosphoacceptor site

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Unique features of HIV-1 Rev protein phosphorylation by protein kinase CK2 (‘casein kinase-2’)

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Mutational Analysis of Residues Implicated in the Interaction between Protein Kinase CK2 and Peptide Substrates†

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Subunit structure and autophosphorylation mechanism of casein kinase-TS (type-2) from rat liver cytosol

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The regulatory beta subunit of protein kinase CK2 mediates formation of tetrameric CK2 complexes

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Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme

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Recombinant human casein kinase II. A study with the complete set of subunits (alpha, alpha' and beta), site-directed autophosphorylation mutants and a bicistronically expressed holoenzyme.

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Phosphorylation of the beta subunit of casein kinase II in human A431 cells. Identification of the autophosphorylation site and a site phosphorylated by p34cdc2.

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Role of the beta subunit of casein kinase-2 on the stability and specificity of the recombinant reconstituted holoenzyme

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Specific binding of protein kinase CK2 catalytic subunits to tubulin

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12 December 2020