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Jumonji domain‐containing protein 6 protein and its role in cancer

The jumonji domain‐containing protein 6 (JMJD6) is a Fe(II)‐ and 2‐oxoglutarate (2OG)‐dependent oxygenase that catalyses lysine hydroxylation and arginine demethylation of histone and non‐histone peptides. Recently, the intrinsic tyrosine kinase activity of JMJD6 has also been reported. The JMJD6 ha...

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Detalles Bibliográficos
Autores principales: Yang, Jing, Chen, Siyuan, Yang, Yanfei, Ma, Xuelei, Shao, Bin, Yang, Shengyong, Wei, Yuquan, Wei, Xiawei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7046477/
https://www.ncbi.nlm.nih.gov/pubmed/31961032
http://dx.doi.org/10.1111/cpr.12747
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author Yang, Jing
Chen, Siyuan
Yang, Yanfei
Ma, Xuelei
Shao, Bin
Yang, Shengyong
Wei, Yuquan
Wei, Xiawei
author_facet Yang, Jing
Chen, Siyuan
Yang, Yanfei
Ma, Xuelei
Shao, Bin
Yang, Shengyong
Wei, Yuquan
Wei, Xiawei
author_sort Yang, Jing
collection PubMed
description The jumonji domain‐containing protein 6 (JMJD6) is a Fe(II)‐ and 2‐oxoglutarate (2OG)‐dependent oxygenase that catalyses lysine hydroxylation and arginine demethylation of histone and non‐histone peptides. Recently, the intrinsic tyrosine kinase activity of JMJD6 has also been reported. The JMJD6 has been implicated in embryonic development, cellular proliferation and migration, self‐tolerance induction in the thymus, and adipocyte differentiation. Not surprisingly, abnormal expression of JMJD6 may contribute to the development of many diseases, such as neuropathic pain, foot‐and‐mouth disease, gestational diabetes mellitus, hepatitis C and various types of cancer. In the present review, we summarized the structure and functions of JMJD6, with particular emphasis on the role of JMJD6 in cancer progression.
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spelling pubmed-70464772020-03-13 Jumonji domain‐containing protein 6 protein and its role in cancer Yang, Jing Chen, Siyuan Yang, Yanfei Ma, Xuelei Shao, Bin Yang, Shengyong Wei, Yuquan Wei, Xiawei Cell Prolif Reviews The jumonji domain‐containing protein 6 (JMJD6) is a Fe(II)‐ and 2‐oxoglutarate (2OG)‐dependent oxygenase that catalyses lysine hydroxylation and arginine demethylation of histone and non‐histone peptides. Recently, the intrinsic tyrosine kinase activity of JMJD6 has also been reported. The JMJD6 has been implicated in embryonic development, cellular proliferation and migration, self‐tolerance induction in the thymus, and adipocyte differentiation. Not surprisingly, abnormal expression of JMJD6 may contribute to the development of many diseases, such as neuropathic pain, foot‐and‐mouth disease, gestational diabetes mellitus, hepatitis C and various types of cancer. In the present review, we summarized the structure and functions of JMJD6, with particular emphasis on the role of JMJD6 in cancer progression. John Wiley and Sons Inc. 2020-01-21 /pmc/articles/PMC7046477/ /pubmed/31961032 http://dx.doi.org/10.1111/cpr.12747 Text en © 2020 The Authors. Cell Proliferation Published by John Wiley & Sons Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Reviews
Yang, Jing
Chen, Siyuan
Yang, Yanfei
Ma, Xuelei
Shao, Bin
Yang, Shengyong
Wei, Yuquan
Wei, Xiawei
Jumonji domain‐containing protein 6 protein and its role in cancer
title Jumonji domain‐containing protein 6 protein and its role in cancer
title_full Jumonji domain‐containing protein 6 protein and its role in cancer
title_fullStr Jumonji domain‐containing protein 6 protein and its role in cancer
title_full_unstemmed Jumonji domain‐containing protein 6 protein and its role in cancer
title_short Jumonji domain‐containing protein 6 protein and its role in cancer
title_sort jumonji domain‐containing protein 6 protein and its role in cancer
topic Reviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7046477/
https://www.ncbi.nlm.nih.gov/pubmed/31961032
http://dx.doi.org/10.1111/cpr.12747
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