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

被引:40
作者
Salvi, Mauro
Sarno, Stefania
Marin, Oriano
Meggio, Flavio
Itarte, Emilio
Pinna, Lorenzo A.
机构
[1] Univ Padua, Dipartimento Chim Biol, I-35121 Padua, Italy
[2] Univ Autonoma Barcelona, Dept Bioquim & Biol Mol, Bellaterra, Barcelona, Spain
来源
FEBS LETTERS | 2006年 / 580卷 / 16期
关键词
CK2 peptide substrate; CK2 activity assay; CK2; holoenzyme;
D O I
10.1016/j.febslet.2006.06.031
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:3948 / 3952
页数:5
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