Abstract
Jumonji domain-containing protein 6 (JMJD6) is a non-heme Fe(II) 2-oxoglutarate (2OG)-dependent oxygenase with arginine demethylase and lysyl hydroxylase activities. Its initial discovery as a dispensable phosphatidylserine receptor (PSR) in the cell membrane of macrophages for phagocytosis was squashed by newer studies which revealed its nuclear localization and bifunctional enzymatic activity. Though its interaction with several nuclear and cytoplasmic target proteins has been demonstrated, the exact mechanisms and clinical significance of these various biologic interplays are not yet well established. Recent investigations have shed the light on the multiple pathways by which JMJD6 can regulate cell proliferation and cause tumorigenesis. Clinically, JMJD6 has been associated with more aggressive and metastatic disease, poorer prognosis, and lower overall survival rates—particularly in lung colon and oral cancers. JMJD6 is a novel biomarker for predicting future disease outcomes and is a target for new therapeutic treatments in future studies. Aberrant expression and dysregulation of JMJD6 are implicated in various other processes such as impaired T-cell proliferation and maturation, inoculation, and virulence of foot-and-mouth disease virus (FMDV), and impaired methylation of innate immunity factor. This article reviews the association of JMJD6 with various pathological processes—particularly, its role in tumorigenesis and virological interactions.
Highlights
In the early 1960s, protein methylation was first described with the discovery of ε-N-methyl-lysine in the flagellar protein of Salmonella typhimurium [1]
The core protein structural fold i.e., double-stranded B-helix (DSBH) is such as three nuclear localization signals (NLS), a DNA binding domain (AT-hook), a putative surrounded by secondary structure
We review the role of JMJD6 in selected cancers
Summary
In the early 1960s, protein methylation was first described with the discovery of ε-N-methyl-lysine in the flagellar protein of Salmonella typhimurium [1]. S-Adenosyl Methionine (SAM) serves as a major methyl donor for many of the transmethylation reactions These reactions are, in turn, catalyzed by a diverse set of methyltransferases resulting in the production of methylated biomolecules such as phospholipids, proteins, nucleic acids, and other small. Histone methyltransferases catalyze the transfer of methyl groups to arginine and lysine residues of histone proteins [16,17], while DNA/RNA methyltransferases primarily methylate the 5-carbon of the base cytosine of DNA [18]. Both types of methyltransferases were extensively investigated because of their direct and indirect role in epigenetic modification of chromatin. We summarize the basic concepts about JMJD6 emphasizing the history, structure, function, and a few known clinical associations—its role in tumorigenesis and virological interactions
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