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.
Highlights
The term “epigenetics” was first conceived by Conrad H
This study reported that Jumonji domain-containing protein 6 (JMJD6) can hydroxylate multiple lysine residues of histone H3 and H4.51 It indicates that in addition to the only known lysyl hydroxylases, the procollagen lysyl hydroxylase (PLOD enzymes), JMJD6 functions as a specialized lysyl hydroxylase
The discovery of JMJD6 as arginine demethylase, lysyl hydroxylase and tyrosine kinase of histone suggests that the protein plays a role in chromatin configuration and epigenetic regulation
Summary
The term “epigenetics” was first conceived by Conrad H.
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