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Closed Access item Kinetic Properties of p53 Phosphorylation by the Human Vaccinia-Related Kinase 1
Vega, Francisco M.
Lazo, Pedro A.
|Citation:||Arch. Biochem. Biophys. 399: 1-5 (2002)|
|Abstract:||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 (Km 50 M) 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 Km of 1 M and is
well suited to respond to the variations of intracellular
p53 concentration, which fluctuates as a response
to different types of cellular stress|
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