Billingsley M L, Kincaid R L
Department of Pharmacology, Pennsylvania State University College of Medicine, 500 University Drive, Hershey, PA 17033, USA.
Biochem J. 1997 May 1;323 ( Pt 3)(Pt 3):577-91. doi: 10.1042/bj3230577.
This review attempts to summarize what is known about tau phosphorylation in the context of both normal cellular function and dysfunction. However, conceptions of tau function continue to evolve, and it is likely that the regulation of tau distribution and metabolism is complex. The roles of microtubule-associated kinases and phosphatases have yet to be fully described, but may afford insight into how tau phosphorylation at the distal end of the axon regulates cytoskeletal-membrane interactions. Finally, lipid and glycosaminoglycan modification of tau structure affords yet more complexity for regulation and aggregation. Continued work will help to determine what is causal and what is coincidental in Alzheimer's disease, and may lead to identification of therapeutic targets for halting the progression of paired helical filament formation.
本综述试图总结在正常细胞功能和功能障碍背景下已知的关于tau蛋白磷酸化的信息。然而，tau蛋白功能的概念仍在不断演变，tau蛋白分布和代谢的调节可能很复杂。微管相关激酶和磷酸酶的作用尚未完全阐明，但可能有助于深入了解轴突末端的tau蛋白磷酸化如何调节细胞骨架与膜的相互作用。最后，tau蛋白结构的脂质和糖胺聚糖修饰为调节和聚集带来了更多复杂性。持续的研究将有助于确定在阿尔茨海默病中哪些是因果关系，哪些是巧合，并可能导致识别出阻止双螺旋丝形成进展的治疗靶点。
