JMJD6

Official Full Name

jumonji domain containing 6, arginine demethylase and lysine hydroxylase

Organism

Homo sapiens

GeneID

23210

Background

This gene encodes a nuclear protein with a JmjC domain. JmjC domain-containing proteins are predicted to function as protein hydroxylases or histone demethylases. This protein was first identified as a putative phosphatidylserine receptor involved in phagocytosis of apoptotic cells; however, subsequent studies have indicated that it does not directly function in the clearance of apoptotic cells, and questioned whether it is a true phosphatidylserine receptor. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

Synonyms

PSR; PTDSR; PTDSR1;

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Detailed Information

Recent Research

JMJD6 is a member of the Jumonji C domain-containing family of proteins. JMJD6 was a phosphatidylserine receptor on cell membrane functioning in phagocytosis of apoptotic cells. Moreover, Jmjd6 is one of the Fe (II) and 2-oxoglutarate (2OG) dependent oxygenase family. The Jmjd6 protein is highly conserved in the animal kingdom and plays an essential role in embryonic development. Some reports show that Jmjd6-knock-out results in serious developmental defects, e.g. in heart and brain and embryos died prenatally. Jmjd6 has also been reported to modify histones, the bromodomain containing protein Brd4 and the tumor suppressor p53. Jmjd6 was reported to be the arginine/serinerich (RS-) domains of U2AF65, SRSF11, Luc7L3 and Acinus S. There is a major function of Jmjd6 in splicing modulation and that this is achieved principally via its interaction with RS domains of SR-like proteins.

JMJD6 is physically associated with the tumor suppressor p53. Knockdown of JMJD6 inhibits p53-dependent colon cell proliferation and tumorigenesis in vivo. JMJD6 antagonizes p53 acetylation, promotes the association of p53 with its negative regulator MDMX, and represses transcriptional activity of p53. Furthermore, expression of JMJD6 is significantly up-regulated in various types of human cancer especially in colon cancer, and high nuclear JMJD6 protein is strongly associated with aggressive clinical behaviors of colon adenocarcinomas. Depletion of JMJD6 enhances transcriptional activity of p53, prevents cells into the G1 phase, promotes cell apoptosis, and sensitizes cells to DNA damaging agent-induced cell death. JMJD6 overexpresses in various human cancers and that high nuclear JMJD6 protein is involved in aggressive clinical behaviors of colon adenocarcinomas. JMJD6 target proteins are involved in different mRNA processing steps and play roles in exon dependent alternative splicing and exon definition. High expression of JMJD6 was associated with poor disease-free survival of patients. JMJD6 silencing in breast tumoural cells promotes certain characteristics of tumorigenesis including proliferation, migration in vitro and tumor growth in vivo.

JMJD6 demethylates the ERa methylated on R260, thereby regulating oestrogen non-genomic signalling.JMJD6 regulates other arginine methylated-proteins. JMJD6 possesses catalytic activity as dioxygenase in the nucleus. JMJD6 was capable of demethylating histone H3 at arginine 2 (H3R2) and histone H4 at arginine 3 (H4R3). The demethylase activity of JMJD6 is a decisive regulator of the rapid physiological responses to oestrogen.JMJD6 possesses lysylhydroxydase activity.JMJD6 remove the methyl moieties on histone H3 at arginine 2 (H3R2) and histone H4 at arginine 3 (H4R3) or as a lysyl hydroxylase to target U2AF65, a protein associated with RNA splicing. JMJD6 demethylates a non-histone substrate, the oestrogen receptor alpha, in which methylation regulates the non-genomic signalling of oestrogens. Jmjd6 plays a role in the regulation of pre-mRNA processing and interacts with multiple arginine–serine-rich (RS)-domains of SR- and SR related proteins including U2AF65, Luc7-like protein 3 (Luc7L3), SRSF11 and Acinus S, but not with the bona fide RS-domain of SRSF1. Jmjd6 target proteins are involved in different mRNA processing steps and play roles in exon dependent alternative splicing and exon definition. In mouse endothelial cells where Jmjd6 knockdown changed splicing of the vascular endothelial growth factor (VEGF)-receptor Flt1 pre-mRNA and thereby promoted expression of a soluble form of the receptor, which inhibits angiogenesis by binding to VEGF.

References:

Wang F, et al. JMJD6 Promotes Colon Carcinogenesis through Negative Regulation of p53 by Hydroxylation. Plos Biology, 2014, 12(3):e1001819.
Poulard C, et al. JMJD6 regulates ERalpha methylation on arginine. Plos One, 2014, 9(2):e87982.
Chen C F, et al. Regulation of T cell proliferation by JMJD6 and PDGF-BB during chronic hepatitis B infection. Scientific Reports, 2014, 4:6359.
Poulard C, et al. Role of JMJD6 in Breast Tumourigenesis. 2015, 10(5):e0126181.
Heim A, et al. Jumonji domain containing protein 6 (Jmjd6) modulates splicing and specifically interacts with arginine–serine-rich (RS) domains of SR- and SR-like proteins. Nucleic Acids Research, 2014, 42(12):7833-7850.

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