JMJD6: A Potential Drug Target for Cancer and Other Diseases (G23210)

Target Name: JMJD6

NCBI ID: G23210

JMJD6: A Potential Drug Target for Cancer and Other Diseases

Histone modifications play a crucial role in the regulation of gene expression and are involved in many cellular processes, including cell growth, differentiation, and response to stimuli. The histone arginine demethylase (JMJD6) is an enzyme that modifies the arginine residue on the histone tails, and is involved in the histone code. In this article, we will discuss the JMJD6 enzyme, its function, and its potential as a drug target.

Function of JMJD6

JMJD6 is an enzyme that belongs to the superfamily of arginine-modifying enzymes known as ADEHs (Arginine DNA Methylase). This family of enzymes includes also the well-known ADEH1 enzyme, which is involved in the regulation of gene expression by DNA methylation. JMJD6 is characterized by its catalytic mechanism, which involves the use of a specific active site to histone arginine demethylase.

The catalytic mechanism of JMJD6 involves the use of a specific active site on the histone tails, where the enzyme binds to the protein and modifies the arginine residue. The active site is a region of the protein that is specific for the JMJD6 enzyme and contains a conserved core that is involved in the binding of the enzyme to the histone tails.

In addition to its role in modifying the arginine residue, JMJD6 also plays an important role in the regulation of cellular processes, including cell growth, differentiation, and response to stimuli. JMJD6 has been shown to play a role in the regulation of cell growth by controlling the cell cycle progression.

Potential as a Drug Target

JMJD6 has been identified as a potential drug target due to its involvement in the regulation of cellular processes and its unique catalytic mechanism. The development of drugs that target JMJD6 has the potential to treat a variety of diseases, including cancer, neurodegenerative diseases, and autoimmune diseases.

One of the reasons for the potential of JMJD6 as a drug target is its involvement in the regulation of cell growth and the use of JMJD6 inhibitors could potentially slow down or stop the growth of cancer cells. Additionally, JMJD6 has been shown to play a role in the regulation of differentiation and has been used to treat diseases that are characterized by the failure of differentiate cells to maintain their normal functions.

Another potential mechanism by which JMJD6 can be targeted is its role in the regulation of cellular response to stimuli. JMJD6 has been shown to play a role in the regulation of inflammation and has been used to treat diseases that are characterized by inflammation.

Conclusion

JMJD6 is an enzyme that is involved in the regulation of many cellular processes and has the potential to be a drug target for the treatment of a variety of diseases. The development of drugs that target JMJD6 has the potential to improve our understanding of the disease mechanisms and to develop new treatments. Further research is needed to fully understand the role of JMJD6 in cellular processes and to develop effective treatments.

Protein Name: Jumonji Domain Containing 6, Arginine Demethylase And Lysine Hydroxylase

Functions: Dioxygenase that can both act as a arginine demethylase and a lysyl-hydroxylase (PubMed:24498420, PubMed:17947579, PubMed:20684070, PubMed:21060799, PubMed:22189873). Acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Regulates RNA splicing by mediating 5-hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65 (PubMed:19574390). Hydroxylates its own N-terminus, which is required for homooligomerization (PubMed:22189873). In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by its ability to bind single strand RNA (PubMed:20679243, PubMed:29176719). Also acts as an arginine demethylase which preferentially demethylates asymmetric dimethylation (PubMed:17947579, PubMed:24498420, PubMed:24360279). Demethylates histone H3 at 'Arg-2' (H3R2me) and histone H4 at 'Arg-3' (H4R3me), including mono-, symmetric di- and asymmetric dimethylated forms, thereby playing a role in histone code (PubMed:17947579, PubMed:24360279). However, histone arginine demethylation may not constitute the primary activity in vivo (PubMed:17947579, PubMed:21060799, PubMed:22189873). In collaboration with BRD4, interacts with the positive transcription elongation factor b (P-TEFb) complex in its active form to regulate polymerase II promoter-proximal pause release for transcriptional activation of a large cohort of genes. On distal enhancers, so called anti-pause enhancers, demethylates both histone H4R3me2 and the methyl cap of 7SKsnRNA leading to the dismissal of the 7SKsnRNA:HEXIM1 inhibitor complex. After removal of repressive marks, the complex BRD4:JMJD6 attract and retain the P-TEFb complex on chromatin, leading to its activation, promoter-proximal polymerase II pause release, and transcriptional activation (PubMed:24360279). Demethylates other arginine methylated-proteins such as ESR1 (PubMed:24498420). Has no histone lysine demethylase activity (PubMed:21060799). Required for differentiation of multiple organs during embryogenesis. Acts as a key regulator of hematopoietic differentiation: required for angiogenic sprouting by regulating the pre-mRNA splicing activity of U2AF2/U2AF65 (By similarity). Seems to be necessary for the regulation of macrophage cytokine responses (PubMed:15622002)

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