Dissecting subdomains involved in multiple functions of the CK2β subunit View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1999

AUTHORS

Didier Leroy , Odile Filhol , Nora Quintaine , Denis Sarrouilhe , Petra Loue-Mackenbach , Edmond M. Chambaz , Claude Cochet

ABSTRACT

We have characterized several subdomains of the β subunit of protein kinase CK2. The N-terminal half of the protein exhibits a pseudo-substrate segment in tandem with a polyamine binding domain responsible for the activation of the kinase by these polybasic compounds. Study of the chemical features of this polyamine binding site showed that polyamine analogs exhibiting the highest affinity for CK2 are the best CK2 activators. Mutational analysis disclosed that glutamic residues lying in the polyacidic region of the CK2β subunit are involved in the interaction with polyamine molecules and allowed the delineation of an autonomous binding domain. Furthermore, this regulatory domain was shown to mediate the association of CK2 with plasma membrane. The C-terminal domain of the CK2β subunit plays a role in the oligomerization of the kinase since it was observed that a truncated form of this subunit lacking its 33-last amino acids was incompetent for the assembly of polymeric forms of CK2. Altogether, our results support the notion that the β subunit of CK2 is a modular protein made by the association of interdependent domains that are involved in its multiple functions. (Mol Cell Biochem 191: 43–50, 1999) More... »

PAGES

43-50

Book

TITLE

A Molecular and Cellular View of Protein Kinase CK2

ISBN

978-1-4613-4648-7
978-1-4419-8624-5

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4419-8624-5_6

DOI

http://dx.doi.org/10.1007/978-1-4419-8624-5_6

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1012996951


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