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Proline-Rich Protein Tyrosine Kinase 2 in Inflammation and Cancer
Focal adhesion kinase (FAK) and its homologous FAK-related proline-rich tyrosine kinase 2 (Pyk2) contain the same domain, exhibit high sequence homology and are defined as a distinct family of non-receptor tyrosine kinases. This group of kinases plays critical roles in cytoskeletal dynamics and cell...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5977112/ https://www.ncbi.nlm.nih.gov/pubmed/29738483 http://dx.doi.org/10.3390/cancers10050139 |
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author | Zhu, Xiangdong Bao, Yonghua Guo, Yongchen Yang, Wancai |
author_facet | Zhu, Xiangdong Bao, Yonghua Guo, Yongchen Yang, Wancai |
author_sort | Zhu, Xiangdong |
collection | PubMed |
description | Focal adhesion kinase (FAK) and its homologous FAK-related proline-rich tyrosine kinase 2 (Pyk2) contain the same domain, exhibit high sequence homology and are defined as a distinct family of non-receptor tyrosine kinases. This group of kinases plays critical roles in cytoskeletal dynamics and cell adhesion by regulating survival and growth signaling. This review summarizes the physiological and pathological functions of Pyk2 in inflammation and cancers. In particular, overexpression of Pyk2 in cancerous tissues is correlated with poor outcomes. Pyk2 stimulates multiple oncogenic signaling pathways, such as Wnt/β-catenin, PI3K/Akt, MAPK/ERK, and TGF-β/EGFR/VEGF, and facilitates carcinogenesis, migration, invasion, epithelial–mesenchymal transition and metastasis. Therefore, Pyk2 is a high-value therapeutic target and has clinical significance. |
format | Online Article Text |
id | pubmed-5977112 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-59771122018-05-31 Proline-Rich Protein Tyrosine Kinase 2 in Inflammation and Cancer Zhu, Xiangdong Bao, Yonghua Guo, Yongchen Yang, Wancai Cancers (Basel) Review Focal adhesion kinase (FAK) and its homologous FAK-related proline-rich tyrosine kinase 2 (Pyk2) contain the same domain, exhibit high sequence homology and are defined as a distinct family of non-receptor tyrosine kinases. This group of kinases plays critical roles in cytoskeletal dynamics and cell adhesion by regulating survival and growth signaling. This review summarizes the physiological and pathological functions of Pyk2 in inflammation and cancers. In particular, overexpression of Pyk2 in cancerous tissues is correlated with poor outcomes. Pyk2 stimulates multiple oncogenic signaling pathways, such as Wnt/β-catenin, PI3K/Akt, MAPK/ERK, and TGF-β/EGFR/VEGF, and facilitates carcinogenesis, migration, invasion, epithelial–mesenchymal transition and metastasis. Therefore, Pyk2 is a high-value therapeutic target and has clinical significance. MDPI 2018-05-08 /pmc/articles/PMC5977112/ /pubmed/29738483 http://dx.doi.org/10.3390/cancers10050139 Text en © 2018 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Zhu, Xiangdong Bao, Yonghua Guo, Yongchen Yang, Wancai Proline-Rich Protein Tyrosine Kinase 2 in Inflammation and Cancer |
title | Proline-Rich Protein Tyrosine Kinase 2 in Inflammation and Cancer |
title_full | Proline-Rich Protein Tyrosine Kinase 2 in Inflammation and Cancer |
title_fullStr | Proline-Rich Protein Tyrosine Kinase 2 in Inflammation and Cancer |
title_full_unstemmed | Proline-Rich Protein Tyrosine Kinase 2 in Inflammation and Cancer |
title_short | Proline-Rich Protein Tyrosine Kinase 2 in Inflammation and Cancer |
title_sort | proline-rich protein tyrosine kinase 2 in inflammation and cancer |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5977112/ https://www.ncbi.nlm.nih.gov/pubmed/29738483 http://dx.doi.org/10.3390/cancers10050139 |
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