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PTEN Dual Lipid- and Protein-Phosphatase Function in Tumor Progression
SIMPLE SUMMARY: Phosphatase and tensin homolog deleted on chromosome ten (PTEN) is a multifunctional tumor suppressor with protein- and lipid-phosphatase activities. The inactivation of PTEN is commonly found in all human cancers and is correlated with tumor progression. PTEN-lipid-phosphatase activ...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9367293/ https://www.ncbi.nlm.nih.gov/pubmed/35954330 http://dx.doi.org/10.3390/cancers14153666 |
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author | Liu, Anne Zhu, Yanyu Chen, Weiping Merlino, Glenn Yu, Yanlin |
author_facet | Liu, Anne Zhu, Yanyu Chen, Weiping Merlino, Glenn Yu, Yanlin |
author_sort | Liu, Anne |
collection | PubMed |
description | SIMPLE SUMMARY: Phosphatase and tensin homolog deleted on chromosome ten (PTEN) is a multifunctional tumor suppressor with protein- and lipid-phosphatase activities. The inactivation of PTEN is commonly found in all human cancers and is correlated with tumor progression. PTEN-lipid-phosphatase activity has been well documented to dephosphorylate phosphatidylinositol-3, 4, 5-phosphate (PIP3), which hinders cell growth and survival by dampening the PI3K and AKT signaling activity. PTEN-protein-phosphatase activity is less well studied and understood. Recent studies have reported that PTEN-protein-phosphatase activity dephosphorylates the different proteins and acts in various cell functions. We here review the PTEN mutations and protein-phosphatase substrates in tumor progression. We aim to address the gap in our understanding as to how PTEN protein phosphatase contributes to its tumor-suppression functions. ABSTRACT: PTEN is the second most highly mutated tumor suppressor in cancer, following only p53. The PTEN protein functions as a phosphatase with lipid- and protein-phosphatase activity. PTEN-lipid-phosphatase activity dephosphorylates PIP3 to form PIP2, and it then antagonizes PI3K and blocks the activation of AKT, while its protein-phosphatase activity dephosphorylates different protein substrates and plays various roles in tumorigenesis. Here, we review the PTEN mutations and protein-phosphatase substrates in tumorigenesis and metastasis. Our purpose is to clarify how PTEN protein phosphatase contributes to its tumor-suppressive functions through PI3K-independent activities. |
format | Online Article Text |
id | pubmed-9367293 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-93672932022-08-12 PTEN Dual Lipid- and Protein-Phosphatase Function in Tumor Progression Liu, Anne Zhu, Yanyu Chen, Weiping Merlino, Glenn Yu, Yanlin Cancers (Basel) Review SIMPLE SUMMARY: Phosphatase and tensin homolog deleted on chromosome ten (PTEN) is a multifunctional tumor suppressor with protein- and lipid-phosphatase activities. The inactivation of PTEN is commonly found in all human cancers and is correlated with tumor progression. PTEN-lipid-phosphatase activity has been well documented to dephosphorylate phosphatidylinositol-3, 4, 5-phosphate (PIP3), which hinders cell growth and survival by dampening the PI3K and AKT signaling activity. PTEN-protein-phosphatase activity is less well studied and understood. Recent studies have reported that PTEN-protein-phosphatase activity dephosphorylates the different proteins and acts in various cell functions. We here review the PTEN mutations and protein-phosphatase substrates in tumor progression. We aim to address the gap in our understanding as to how PTEN protein phosphatase contributes to its tumor-suppression functions. ABSTRACT: PTEN is the second most highly mutated tumor suppressor in cancer, following only p53. The PTEN protein functions as a phosphatase with lipid- and protein-phosphatase activity. PTEN-lipid-phosphatase activity dephosphorylates PIP3 to form PIP2, and it then antagonizes PI3K and blocks the activation of AKT, while its protein-phosphatase activity dephosphorylates different protein substrates and plays various roles in tumorigenesis. Here, we review the PTEN mutations and protein-phosphatase substrates in tumorigenesis and metastasis. Our purpose is to clarify how PTEN protein phosphatase contributes to its tumor-suppressive functions through PI3K-independent activities. MDPI 2022-07-28 /pmc/articles/PMC9367293/ /pubmed/35954330 http://dx.doi.org/10.3390/cancers14153666 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Liu, Anne Zhu, Yanyu Chen, Weiping Merlino, Glenn Yu, Yanlin PTEN Dual Lipid- and Protein-Phosphatase Function in Tumor Progression |
title | PTEN Dual Lipid- and Protein-Phosphatase Function in Tumor Progression |
title_full | PTEN Dual Lipid- and Protein-Phosphatase Function in Tumor Progression |
title_fullStr | PTEN Dual Lipid- and Protein-Phosphatase Function in Tumor Progression |
title_full_unstemmed | PTEN Dual Lipid- and Protein-Phosphatase Function in Tumor Progression |
title_short | PTEN Dual Lipid- and Protein-Phosphatase Function in Tumor Progression |
title_sort | pten dual lipid- and protein-phosphatase function in tumor progression |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9367293/ https://www.ncbi.nlm.nih.gov/pubmed/35954330 http://dx.doi.org/10.3390/cancers14153666 |
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