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.-Reference-Cited by-同舟云学术

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.

Published:1994-02 Issue:7 Volume:269 Page:4827-4831
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Boldyreff B.,Meggio F.,Pinna L.A.,Issinger O.G.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference18 articles.

1. Stimulation of casein kinase II by epidermal growth factor: relationship between the physiological activity of the kinase and the phosphorylation state of its beta subunit.

2. Regulation of casein kinase 2 by phosphorylation/dephosphorylation

3. Phosphorylation of Calmodulin by the Catalytic Subunit of Casein Kinase II Is Inhibited by the Regulatory Subunit

4. Casein kinase-2 structure-function relationship: Creation of a set of mutants of the β subunit that variably surrogate the wildtype β subunit function

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