The antiapoptotic protein ICBP90 is a target for protein kinase 2

被引：10

作者：

Bronner, C

Trotzier, MA

Filhol, O

Cochet, C

Rochette-Egly, C

Schöller-Guinard, M

Klein, JP

Mousli, M

机构：

[1] Fac Pharm, INSERM, UMRS392, F-67401 Illkirch Graffenstaden, France

[2] INSERM, Dept Reponse & Dynam Cellulaire, EMI 104, Commessariat Energie Atom, F-38054 Grenoble, France

[3] INSERM, UMRS596, F-67404 Illkirch Graffenstaden, France

来源：

SIGNAL TRANSDUCTION PATHWAYS, CHROMATIN STRUCTURE, AND GENE EXPRESSION MECHANISMS AS THERAPEUTIC TARGETS | 2004年 / 1030卷

关键词：

apoptosis; cancer; cell proliferation; CK2; ICBP90;

D O I：

10.1196/annals.1329.044

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：

Protein kinase 2 (casein kinase 2 [CK2]) is a protein serine/threonine kinase involved in cell proliferation with an expression that is dysregulated in tumors. ICBP90, a transcription factor exhibiting antiapoptotic properties, has several putative CK2 phosphorylation sites. The aim of the present study was to investigate whether ICBP90 could behave as a CK2 substrate. We observed that ICBP90 was more efficiently phosphorylated by the free CK2 alpha subunit than by the heterotetrameric CK2 (alpha(2), beta(2)). Our results suggest that CK2 is an important regulator of the transcriptional activity of ICBP90 and therefore of the antiapoptotic properties of ICBP90. We propose that the "ICBP90 family" members may be substrates for CK2.

引用

页码：355 / 360

页数：6

共 18 条

[1] ICBP90 expression is downregulated in apoptosis-induced Jurkat cells [J].