Research progress in structure and biological function of protein phosphatase 1 and its relationship with occurence and development of tumor
10.13481/j.1671-587X.20250329
- VernacularTitle:蛋白磷酸酶1结构和生物学功能及其与肿瘤发生发展关系的研究进展
- Author:
Wengxiu GUO
1
;
Huiling ZHANG
;
Jun MENG
Author Information
1. 内蒙古医科大学附属医院临床检验诊断教研室,内蒙古 呼和浩特 010059
- Keywords:
Protein phosphatase 1;
Serine-threonine phosphatase;
Protein phosphatase 1 regulatory proteins;
Biological function;
Dephosphorylation
- From:
Journal of Jilin University(Medicine Edition)
2025;51(3):822-830
- CountryChina
- Language:Chinese
-
Abstract:
Protein phosphatase 1(PP1)is a widely expressed and highly conserved serine/threonine phosphatase in organisms.It regulates cellular signaling pathways by catalyzing the dephosphorylation of various proteins,thereby influencing biological processes such as cell proliferation,apoptosis,migration,and transcription.In vivo,PP1 does not exist as a free catalytic subunit but instead forms distinct PP1 holoenzymes by binding with at least one PP1-interacting protein(PIP).The interaction between PP1's catalytic subunit and its specific regulatory proteins is central to PP1's function.Under normal conditions,PP1 stably performs its dephosphorylation role in vivo;however,in tumors,PP1 function is aberrantly regulated,leading to either increased or decreased PP1 activity.PP1 exerts a dual influence on tumorigenesis and progression,acting as a suppressor in some cancers while promoting oncogenesis in others.Based on domestic and international research findings on PP1,this review summarizes the structure and biological functions of PP1,as well as the impact of its various subunits on the development and progression of different cancers,including breast cancer,lung cancer,ovarian cancer,pancreatic adenocarcinoma(PAAD),liver cancer,endometrial cancer,esophageal cancer(EC),colorectal cancer,and glioblastoma(GBM).This review aims to provide the insights for developing highly efficient and environmentally friendly anticancer drugs and therapeutic approaches targeting PP1 holoenzymes.
