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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Published inCell proliferation Vol. 53; no. 2; pp. e12747 - n/a
Main Authors Yang, Jing, Chen, Siyuan, Yang, Yanfei, Ma, Xuelei, Shao, Bin, Yang, Shengyong, Wei, Yuquan, Wei, Xiawei
Format Journal Article
LanguageEnglish
Published England John Wiley & Sons, Inc 01.02.2020
John Wiley and Sons Inc
Subjects
Adenosine triphosphate
Animals
Arginine
Binding sites
Cancer
Demethylation
Deoxyribonucleic acid
Diabetes mellitus
Diabetic neuropathy
Disease Progression
DNA
DNA methylation
Embryogenesis
Embryonic growth stage
Enzymes
Epigenetics
Gene expression
Hepatitis C
Histones
Humans
Hydroxylation
Immunological tolerance
Iron
JMJD6 protein
Jumonji Domain-Containing Histone Demethylases - metabolism
jumonji domain‐containing histone demethylases
Kinases
Localization
Lysine
Neoplasms - metabolism
Neoplasms - pathology
Oxygenase
Peptides
Protein-tyrosine kinase
Proteins
Review
Reviews
Tyrosine
JMJD6 protein
cancer
jumonji domain-containing histone demethylases
epigenetics
Online AccessGet full text

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Abstract 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.
AbstractList 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.
Abstract 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.
Author Chen, Siyuan
Wei, Xiawei
Wei, Yuquan
Yang, Jing
Ma, Xuelei
Shao, Bin
Yang, Shengyong
Yang, Yanfei
AuthorAffiliation 2 State Key Laboratory of Oral Disease West China Hospital of Stomatology Sichuan University Chengdu Sichuan China
1 Laboratory of Aging Research and Nanotoxicology State Key Laboratory of Biotherapy and Cancer Center National Clinical Research Center for Geriatrics West China Hospital Sichuan University Chengdu Sichuan China
AuthorAffiliation_xml – name: 1 Laboratory of Aging Research and Nanotoxicology State Key Laboratory of Biotherapy and Cancer Center National Clinical Research Center for Geriatrics West China Hospital Sichuan University Chengdu Sichuan China
– name: 2 State Key Laboratory of Oral Disease West China Hospital of Stomatology Sichuan University Chengdu Sichuan China
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  organization: Sichuan University
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2020 The Authors. Cell Proliferation Published by John Wiley & Sons Ltd.
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Issue 2
Keywords JMJD6 protein
cancer
jumonji domain-containing histone demethylases
epigenetics
Language English
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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.
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Notes Funding information
This work is supported by the National Natural Science Foundation of China (No. 81602492), the National Key Research and Development Program of China (No. 2016YFA0201402), the National Major Scientific, Technological Special Project for “Significant New Drugs Development” (No. 2018ZX09733001) and by the Excellent Youth Foundation of Sichuan Scientific Committee Grant in China (No. 2019JDJQ0008).
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Yang, Chen and Ma contributed equally to this work.
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2014; 452‐453
2017; 53
2018; 17
2005; 19
2012; 113
2015; 112
2018; 475
2013; 453
2014; 35
2005; 92
2007; 318
2016; 8
2003; 100
2006; 100
2017; 547
2017; 7
2017; 8
2007; 304
2015; 468
2017; 45
2008; 9
2013; 288
2010; 141
2008; 8
2011; 12
1990; 265
2011; 18
2003; 111
2017; 31
2004; 131
2015; 47
2015; 290
2013; 13
1999; 17
1997; 13
2018; 499
2018; 70
2013; 155
2008; 68
2001; 15
1999; 96
2014; 9
2009; 325
2014; 54
2018; 144
2015; 16
2006; 11
2010; 401
2011; 40
2006; 9
2015; 10
2011; 31
2006; 7
2011; 32
2018; 67
2012; 424
2012; 149
2012; 150
2018; 154
2011; 108
2010; 138
2013; 34
2017; 16
1999; 160
2004; 13
2019
2018; 50
2003; 302
2017; 188
2016; 492
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  doi: 10.1016/S0021-9258(19)38926-4
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Snippet The jumonji domain‐containing protein 6 (JMJD6) is a Fe(II)‐ and 2‐oxoglutarate (2OG)‐dependent oxygenase that catalyses lysine hydroxylation and arginine...
The jumonji domain-containing protein 6 (JMJD6) is a Fe(II)- and 2-oxoglutarate (2OG)-dependent oxygenase that catalyses lysine hydroxylation and arginine...
Abstract The jumonji domain‐containing protein 6 (JMJD6) is a Fe(II)‐ and 2‐oxoglutarate (2OG)‐dependent oxygenase that catalyses lysine hydroxylation and...
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SubjectTerms Adenosine triphosphate
Animals
Arginine
Binding sites
Cancer
Demethylation
Deoxyribonucleic acid
Diabetes mellitus
Diabetic neuropathy
Disease Progression
DNA
DNA methylation
Embryogenesis
Embryonic growth stage
Enzymes
Epigenetics
Gene expression
Hepatitis C
Histones
Humans
Hydroxylation
Immunological tolerance
Iron
JMJD6 protein
Jumonji Domain-Containing Histone Demethylases - metabolism
jumonji domain‐containing histone demethylases
Kinases
Localization
Lysine
Neoplasms - metabolism
Neoplasms - pathology
Oxygenase
Peptides
Protein-tyrosine kinase
Proteins
Review
Reviews
Tyrosine
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Title Jumonji domain‐containing protein 6 protein and its role in cancer
URI https://onlinelibrary.wiley.com/doi/abs/10.1111%2Fcpr.12747
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Volume 53
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