Tuning the Protein Phosphorylation by Receptor Type Protein Tyrosine Phosphatase Epsilon (PTPRE) in Normal and Cancer Cells

Tyrosine phosphorylation is an important post-translation modification of proteins that is controlled by tyrosine kinases and phosphatases. Disruption of the balance between the activity of tyrosine kinases and phosphatases may result in diseases. Receptor type protein tyrosine phosphatase epsilon (...

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Autores principales: Liang, Jinping, Shi, Jun, Wang, Na, Zhao, Hui, Sun, Jianmin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Ivyspring International Publisher 2019
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6329871/
https://www.ncbi.nlm.nih.gov/pubmed/30662530
http://dx.doi.org/10.7150/jca.27633
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author Liang, Jinping
Shi, Jun
Wang, Na
Zhao, Hui
Sun, Jianmin
author_facet Liang, Jinping
Shi, Jun
Wang, Na
Zhao, Hui
Sun, Jianmin
author_sort Liang, Jinping
collection PubMed
description Tyrosine phosphorylation is an important post-translation modification of proteins that is controlled by tyrosine kinases and phosphatases. Disruption of the balance between the activity of tyrosine kinases and phosphatases may result in diseases. Receptor type protein tyrosine phosphatase epsilon (PTPRE) is closely related with receptor type protein tyrosine phosphatase alpha (PTPRA). PTPRE has been studied in osteoclast cells, nerve cells, hematopoietic cells, cancer cells and others, and it has different functions among various tissues. In this review, we summarized the current knowledge about the regulation of PTPRE on cellular signal transduction and its function under normal and pathological conditions.
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spelling pubmed-63298712019-01-18 Tuning the Protein Phosphorylation by Receptor Type Protein Tyrosine Phosphatase Epsilon (PTPRE) in Normal and Cancer Cells Liang, Jinping Shi, Jun Wang, Na Zhao, Hui Sun, Jianmin J Cancer Review Tyrosine phosphorylation is an important post-translation modification of proteins that is controlled by tyrosine kinases and phosphatases. Disruption of the balance between the activity of tyrosine kinases and phosphatases may result in diseases. Receptor type protein tyrosine phosphatase epsilon (PTPRE) is closely related with receptor type protein tyrosine phosphatase alpha (PTPRA). PTPRE has been studied in osteoclast cells, nerve cells, hematopoietic cells, cancer cells and others, and it has different functions among various tissues. In this review, we summarized the current knowledge about the regulation of PTPRE on cellular signal transduction and its function under normal and pathological conditions. Ivyspring International Publisher 2019-01-01 /pmc/articles/PMC6329871/ /pubmed/30662530 http://dx.doi.org/10.7150/jca.27633 Text en © Ivyspring International Publisher This is an open access article distributed under the terms of the Creative Commons Attribution (CC BY-NC) license (https://creativecommons.org/licenses/by-nc/4.0/). See http://ivyspring.com/terms for full terms and conditions.
spellingShingle Review
Liang, Jinping
Shi, Jun
Wang, Na
Zhao, Hui
Sun, Jianmin
Tuning the Protein Phosphorylation by Receptor Type Protein Tyrosine Phosphatase Epsilon (PTPRE) in Normal and Cancer Cells
title Tuning the Protein Phosphorylation by Receptor Type Protein Tyrosine Phosphatase Epsilon (PTPRE) in Normal and Cancer Cells
title_full Tuning the Protein Phosphorylation by Receptor Type Protein Tyrosine Phosphatase Epsilon (PTPRE) in Normal and Cancer Cells
title_fullStr Tuning the Protein Phosphorylation by Receptor Type Protein Tyrosine Phosphatase Epsilon (PTPRE) in Normal and Cancer Cells
title_full_unstemmed Tuning the Protein Phosphorylation by Receptor Type Protein Tyrosine Phosphatase Epsilon (PTPRE) in Normal and Cancer Cells
title_short Tuning the Protein Phosphorylation by Receptor Type Protein Tyrosine Phosphatase Epsilon (PTPRE) in Normal and Cancer Cells
title_sort tuning the protein phosphorylation by receptor type protein tyrosine phosphatase epsilon (ptpre) in normal and cancer cells
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6329871/
https://www.ncbi.nlm.nih.gov/pubmed/30662530
http://dx.doi.org/10.7150/jca.27633
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