Abstract
The Phosphatase and tensin homolog (PTEN) gene is one of the most important tumor suppressor genes, which acts through its unique protein phosphatase and lipid phosphatase activity. PTEN protein is widely distributed and exhibits complex biological functions and regulatory modes. It is involved in the regulation of cell morphology, proliferation, differentiation, adhesion, and migration through a variety of signaling pathways. The role of PTEN in malignant tumors of the digestive system is well documented. Recent studies have indicated that PTEN may be closely related to many other benign processes in digestive organs. Emerging evidence suggests that PTEN is a potential therapeutic target in the context of several non-neoplastic diseases of the digestive tract. The recent discovery of PTEN isoforms is expected to help unravel more biological effects of PTEN in non-neoplastic digestive diseases.
Highlights
Phosphatase and tensin homolog (PTEN) gene, located on chromosome 10q23, was identified as a tumor suppressor gene approximately 20 years ago (Li et al, 1997)
Phosphorylation of PTEN at residues Ser380/Thr382/383 induced by H. pylori was found to promote the survival of gastric epithelial cells, since the phosphorylation of PTEN leads to the loss of phosphatase activity and activation of the phosphatidylinositol 3-kinase (PI3K)/AKT pathway (Yang et al, 2015)
The results demonstrated that the binding of IRS 1 and 2 (IRS1/2) and the endosomal insulin receptor (INSR) can promote insulin receptor substrate-1 (IRS1)/2 phosphorylation and initiate downstream Akt2/glycogen synthase kinase (GSK)-3β and FoxO1 signaling in the liver (Zhang et al, 2020)
Summary
Phosphatase and tensin homolog (PTEN) gene, located on chromosome 10q23, was identified as a tumor suppressor gene approximately 20 years ago (Li et al, 1997). Since PTEN modulates a variety of biological processes, an increasing number of studies have investigated the changes in PTEN in the context of non-neoplastic digestive diseases such as hepatitis, colitides, pancreatitis, hepatic insulin resistance, and liver fibrosis. These studies have partially unraveled the potential role of PTEN and its dual phosphatase activity in non-neoplastic digestive diseases and the associated underlying mechanisms. Dephosphorylation of the PTEN-tail, which confers it a more open conformation, was shown to allow dimerization and stabilize the homo-dimer (Heinrich et al, 2015) These findings provide insights into the cellular function and the molecular mechanism of PTEN activity regulation, which may provide a novel approach for cancer prevention and treatment
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