Tait Andrew R, Straus Suzana K
Department of Chemistry, University of British Columbia, 2036 Main Mall, Vancouver, BC, Canada V6T 1Z1.
FEBS Lett. 2008 Aug 6;582(18):2685-8. doi: 10.1016/j.febslet.2008.06.050. Epub 2008 Jul 9.
Myelin basic protein (MBP) from multiple sclerosis (MS) patients contains lower levels of phosphorylation at Thr97 than normal individuals. The significance of phosphorylation at this site is not fully understood, but it is proposed to play a role in the normal functioning of MBP. Human Herpesvirus Type 6 encodes the protein U24, which has tentatively been implicated in the pathology of MS. U24 shares a 7 amino acid stretch encompassing the Thr97 phosphorylation site of MBP: PRTPPPS. We demonstrate using a combination of mass spectrometry, thin layer chromatography and autoradiography, that U24 can be phosphorylated at the equivalent threonine. Phospho-U24 may confound signalling or other pathways in which phosphorylated MBP may participate, precipitating a pathological process.
来自多发性硬化症（MS）患者的髓鞘碱性蛋白（MBP）在苏氨酸97位点的磷酸化水平低于正常个体。该位点磷酸化的意义尚未完全明确，但据推测其在MBP的正常功能中发挥作用。人疱疹病毒6型编码蛋白U24，初步研究表明该蛋白与MS的病理过程有关。U24有一段包含MBP苏氨酸97磷酸化位点的7个氨基酸序列：PRTPPPS。我们通过质谱分析、薄层色谱法和放射自显影相结合的方法证明，U24在对应的苏氨酸位点可以被磷酸化。磷酸化的U24可能会干扰磷酸化MBP可能参与的信号传导或其他途径，从而引发病理过程。
