Kinetic properties of p53 phosphorylation by the human vaccinia-related kinase 1

被引：46

作者：

Barcia, R ^{[1
]}

López-Borges, S ^{[1
]}

Vega, FM ^{[1
]}

Lazo, PA ^{[1
]}

机构：

[1] Univ Salamanca, Consejo Super Invest Cientificas, Ctr Invest Canc, Inst Biol Mol & Celular Canc, E-37007 Salamanca, Spain

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 2002年 / 399卷 / 01期

关键词：

VRK1; p53; serine-threonine kinase; enzyme activity;

D O I：

10.1006/abbi.2001.2746

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 vaccinia-related kinase 1 (VRK1) protein is a nuclear Ser-Thr kinase that phosphorylates p53 in Thr18. We have determined the enzyme properties regarding its different substrates. VRK1 has a high affinity for ATP (K-m 50 muM) and is thus saturated by the intracellular concentration of ATP in vivo. VRK1 uses preferentially magnesium, but is also functional with manganese and zinc. The VRK1 protein is autophosphorylated in multiple residues without effect on its activity. One autophosphorylated residue, T355, is within the VRK1 regulatory carboxy terminus. The kinase phosphorylates p53 with a K-m of 1 muM and is well suited to respond to the variations of intracellular p53 concentration, which fluctuates as a response to different types of cellular stress. (C) 2002 Elsevier Science (USA).

引用

页码：1 / 5

页数：5

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