蛋白磷酸酶2A在真菌细胞中的研究进展

蛋白质可逆的磷酸化修饰在真菌细胞生命活动中发挥着重要作用。磷酸化与去磷酸化过程相互协调。蛋白质中磷酸丝氨酸/苏氨酸位点的去磷酸化反应主要由蛋白磷酸酶2A (Protein Phosphatase2A,PP2A)负责催化。PP2A由催化亚基、调节亚基与结构亚基组合成有活性的三聚体全酶形式发挥功能。本文以模式真菌酿酒酵母、裂殖酵母与人类条件致病菌白色念珠菌为例,总结了PP2A家族成员在真菌细胞中的研究进展及去磷酸化作用调控真菌细胞生命活动的重要性,分析了PP2A调控真菌生命活动尚需解析的作用机制,并提出了可能的研究思路。

Research progress of fungal protein phosphatase 2A

The reversible phosphorylation modification of protein plays a crucial role in the life activities of fungal cells. The phosphorylation and dephosphorylation processes are coordinated with each other. The dephosphorylation of serine/threonine sites in protein is mainly catalyzed by protein phosphatase 2A (PP2A). The catalytic subunit, regulatory subunit and structural subunit are combined into an active trimeric holoenzyme form when PP2A is functioning. This article will take the model fungi Saccharomyces cerevisiae, Schizosaccharomyces cerevisiae, and the human conditional pathogen Candida albicans as examples to introduce the research progress of PP2A in fungal cells, helpful to understand the importance of dephosphorylation in regulating their life. In addition, we also analyzed the unclear problems in the research field of PP2A, and proposed possible research ideas.