4.5 Article

Discrimination between the activity of protein kinase CK2 holoenzyme and its catalytic subunits

Journal

FEBS LETTERS
Volume 580, Issue 16, Pages 3948-3952

Publisher

WILEY
DOI: 10.1016/j.febslet.2006.06.031

Keywords

CK2 peptide substrate; CK2 activity assay; CK2 holoenzyme

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The acronym CK2 denotes a highly pleiotropic Ser/Thr protein kinase whose over-expression correlates with neoplastic growth. A vexed question about the enigmatic regulation of CK2 concerns the actual existence in living cells of the catalytic (alpha and/or alpha') and regulatory beta-subunits of CK2 not assembled into the regular heterotetrameric holoenzyme. Here we take advantage of novel reagents, namely a peptide substrate and an inhibitor which discriminate between the holoenzyme and the catalytic subunits, to show that CK2 activity in CHO cells is entirely accounted for by the holoenzyme. Transfection with individual subunits moreover does not give rise to holoenzyme formation unless the catalytic and regulatory subunits are cotransfected together, arguing against the existence of free subunits in CHO cells. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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