The reversible phosphorylation of proteins,orchestrated by protein kinases and phosphatases,plays a pivotal role in various life processes.Among these,protein phosphatase 2A(PP2A)is a crucial class of serine/threonine protein phosphatases within the phosphatase family and catalyzes the dephos-phorylation of proteins.The catalytic subunit(C subunit,PP2Ac)and the structural subunit(A subunit,PP2Aa)of PP2A form a dimer,constituting the core complex,which further interacts with a diverse array of regulatory subunits(B subunits,PP2Ab)to form a trimeric holoenzyme complex that exerts its func-tions.This paper primarily discusses the structural characteristics and subcellular localization of PP2A in plants,summarizing recent research progress in its involvement in plant development,hormone signal transduction,and responses to abiotic stress.Investigating the structural features and functions of PP2A contributes to an enhanced understanding of the fine-tuning involved in plant growth,development,and environmental adaptation mediated by this phosphatase.Additionally,it provides a reference for elucidat-ing the role of PP2A in regulating various physiological processes.
万方数据
维普
