Elliott G, O'Reilly D, O'Hare P
Virus Assembly Group, Marie Curie Research Institute, Oxted, Surrey RH1 OTL, United Kingdom.
J Virol. 1999 Jul;73(7):6203-6. doi: 10.1128/JVI.73.7.6203-6206.1999.
The herpes simplex virus protein VP22 is a major phosphoprotein of infected cells. In this study, we identify two serine phosphorylation sites within VP22 and show that the N-terminal site is a substrate for casein kinase II, while the extreme C-terminal site is a substrate for another, as yet unidentified, cellular kinase. Furthermore, we show that a mutant of VP22 which has both sites altered is unable to incorporate phosphate in vivo, confirming that there are no other phosphorylation sites within VP22.
单纯疱疹病毒蛋白VP22是受感染细胞的一种主要磷蛋白。在本研究中，我们鉴定出VP22内的两个丝氨酸磷酸化位点，并表明N端位点是酪蛋白激酶II的底物，而最末端的C端位点是另一种尚未鉴定的细胞激酶的底物。此外，我们表明两个位点均发生改变的VP22突变体在体内无法掺入磷酸盐，这证实了VP22内不存在其他磷酸化位点。
