Recent findings have garnered a substantial amount of attention toward tau based on its pathological contribution to neurodegenerative diseases, such as Alzheimer’s disease (AD). Studies investigating the structure and aggregation of tau under various in vitro and in vivo conditions have revealed its intrinsically disordered structures and amyloidogenesis process. The aggregation behavior of tau is strongly dependent on the experimental conditions due to the high sensitivity of both the soluble tau conformations and the amyloid nucleation process toward its surrounding environments. Herein, we review and discuss (1) the effects of different physicochemical and biological factors as well as intermolecular interactions with various molecular chaperones on tau aggregation, (2) context-dependent liquid-liquid phase separation of tau and its amyloidogenic transformation, and (3) the utility of the phase diagram in comprehending the phase transition and separation of proteins.

基于tau对神经退行性疾病（例如阿尔茨海默氏病（AD））的病理贡献，最近的发现引起了人们对tau的广泛关注。研究各种体外和体内tau的结构和聚集的研究条件已经揭示出其固有的无序结构和淀粉样蛋白生成过程。由于可溶性tau构象和淀粉样蛋白成核过程对周围环境的高度敏感性，tau的聚集行为很大程度上取决于实验条件。在本文中，我们回顾和讨论（1）不同理化和生物学因素以及与各种分子伴侣的分子间相互作用对tau聚集的影响;（2）tau的上下文相关液-液相分离及其淀粉样变性转化;以及（ 3）相图在理解蛋白质的相变和分离中的用途。