Lee V M
Department of Pathology and Laboratory Medicine, University of Pennsylvania School of Medicine, Philadelphia 19104-4283, USA.
Curr Opin Neurobiol. 1995 Oct;5(5):663-8. doi: 10.1016/0959-4388(95)80073-5.
Paired helical filaments (PHFs) in Alzheimer's disease are formed from hyperphosphorylated brain tau known as PHF-tau. Many sites of phosphorylation that were thought to be present only in PHF-tau are now known to be normal phosphate acceptor sites in both fetal and rapidly processed adult brain tau. The rapid dephosphorylation of normal brain tau by protein phosphatases 2A and 2B provides an explanation for the apparent absence of phosphates at these sites in the normal adult brain tau obtained postmortem. Although the functional significance of each of these normal phosphate acceptor sites is unknown at this time, emerging evidence suggests that the binding of tau to microtubules is regulated by the simultaneous phosphorylation and dephosphorylation of tau at multiple sites.
阿尔茨海默病中的双螺旋丝（PHF）由被称为PHF-τ的高度磷酸化脑tau蛋白形成。许多曾被认为仅存在于PHF-τ中的磷酸化位点，如今已知在胎儿和快速处理的成人大脑tau蛋白中都是正常的磷酸受体位点。蛋白磷酸酶2A和2B对正常脑tau蛋白的快速去磷酸化，解释了在死后获得的正常成人大脑tau蛋白中这些位点明显不存在磷酸盐的现象。尽管目前这些正常磷酸受体位点各自的功能意义尚不清楚，但新出现的证据表明，tau蛋白与微管的结合是由tau蛋白在多个位点的同时磷酸化和去磷酸化所调节的。
