Smal C, Ntamashimikiro S, Arts A, Van Den Neste E, Bontemps F
Université Catholique de Louvain, de Duve Institute, Brussels, Belgium.
Nucleosides Nucleotides Nucleic Acids. 2010 Jun;29(4-6):404-7. doi: 10.1080/15257771003741216.
Deoxycytidine kinase (dCK) is a key enzyme in the salvage of deoxyribonucleosides and in the activation of several anticancer and antiviral nucleoside analogues. We have recently shown that dCK is a phosphoprotein. Four in vivo phosphorylation sites were identified: Thr-3, Ser-11, Ser-15, and Ser-74. Site-directed mutagenesis demonstrated that phosphorylation of Ser-74, the major phosphorylated residue, strongly influences dCK activity in eucaryotic cells. Here, we show that phosphorylation of the three other sites, located in the N-terminal extremity of the protein, does not significantly modify dCK activity, but phosphorylation of Thr-3 could promote dCK stability.
脱氧胞苷激酶（dCK）是脱氧核糖核苷补救途径以及多种抗癌和抗病毒核苷类似物激活过程中的关键酶。我们最近发现dCK是一种磷蛋白。已鉴定出四个体内磷酸化位点：苏氨酸-3、丝氨酸-11、丝氨酸-15和丝氨酸-74。定点诱变表明，主要磷酸化残基丝氨酸-74的磷酸化对真核细胞中的dCK活性有强烈影响。在此，我们表明位于该蛋白N末端的其他三个位点的磷酸化不会显著改变dCK活性，但苏氨酸-3的磷酸化可促进dCK的稳定性。
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