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 in | Cell proliferation Vol. 53; no. 2; pp. e12747 - n/a |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
Published |
England
John Wiley & Sons, Inc
01.02.2020
John Wiley and Sons Inc |
Subjects | |
Online Access | Get full text |
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Summary: | 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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Bibliography: | 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). ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 Yang, Chen and Ma contributed equally to this work. |
ISSN: | 0960-7722 1365-2184 |
DOI: | 10.1111/cpr.12747 |