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Identifying interaction motifs in CK2beta--a ubiquitous kinase regulatory subunit.

Authors
Type
Published Article
Journal
Trends in Biochemical Sciences
0968-0004
Publisher
Elsevier
Publication Date
Volume
31
Issue
12
Pages
654–661
Identifiers
PMID: 17084631
Source
Medline
License
Unknown

Abstract

Casein kinase 2 (CK2) is probably the most ubiquitous serine/threonine kinase found in eukaryotes: it phosphorylates >300 cellular proteins, ranging from transcription factors to proteins involved in chromatin structure and cell division. CK2 is a heterotetrameric enzyme that induces neoplastic growth when overexpressed. The beta subunit of CK2 (CK2beta) functions as the regulator of the catalytic CK2alpha and CK2alpha' subunits, enhancing their stability, activity and specificity. However, CK2beta also functions as a multisubstrate docking platform for several other binding partners. Here, we discuss the organization and roles of interaction motifs of CK2beta, postulate new protein-interaction sites and map these to the known interaction motifs, and show how the resulting complexity of interactions mediated by CK2 gives rise to the versatile functions of this pleiotropic protein kinase.

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