Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 is an enzyme that in humans is encoded by the JMJD6gene.[1][2]
Function
This gene encodes a nuclear protein with a JmjC domain. JmjC domain-containing proteins belong to the 2-oxoglutarate (2OG)-dependent dioxygenase superfamily. They 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 suggested that the protein may cross-react with a monoclonal antibody that recognizes the phosphatidylserine receptor and does not directly function in the clearance of apoptotic cells. Multiple transcript variants encoding different isoforms have been found for this gene.[2] JMJD6 has been implicated in mammary tumorigenesis, and it increases breast cancer aggressiveness and metastasis in mice.[3]
Webby CJ, Wolf A, Gromak N, Dreger M, Kramer H, Kessler B, Nielsen ML, Schmitz C, Butler DS, Yates JR, Delahunty CM, Hahn P, Lengeling A, Mann M, Proudfoot NJ, Schofield CJ, Böttger A (July 2009). "Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing". Science. 325 (5936): 90–3. doi:10.1126/science.1175865. PMID19574390.
Zakharova L, Dadsetan S, Fomina AF (October 2009). "Endogenous Jmjd6 gene product is expressed at the cell surface and regulates phagocytosis in immature monocyte-like activated THP-1 cells". Journal of Cellular Physiology. 221 (1): 84–91. doi:10.1002/jcp.21829. PMID19492415.
Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (February 1998). "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Research. 5 (1): 31–9. doi:10.1093/dnares/5.1.31. PMID9628581.
Fadok VA, Bratton DL, Rose DM, Pearson A, Ezekewitz RA, Henson PM (May 2000). "A receptor for phosphatidylserine-specific clearance of apoptotic cells". Nature. 405 (6782): 85–90. doi:10.1038/35011084. PMID10811223.
Ajmone-Cat MA, De Simone R, Nicolini A, Minghetti L (January 2003). "Effects of phosphatidylserine on p38 mitogen activated protein kinase, cyclic AMP responding element binding protein and nuclear factor-kappaB activation in resting and activated microglial cells". Journal of Neurochemistry. 84 (2): 413–6. doi:10.1046/j.1471-4159.2003.01562.x. PMID12559004.
Chan A, Seguin R, Magnus T, Papadimitriou C, Toyka KV, Antel JP, Gold R (September 2003). "Phagocytosis of apoptotic inflammatory cells by microglia and its therapeutic implications: termination of CNS autoimmune inflammation and modulation by interferon-beta". Glia. 43 (3): 231–42. doi:10.1002/glia.10258. PMID12898702.
Wang X, Wu YC, Fadok VA, Lee MC, Gengyo-Ando K, Cheng LC, Ledwich D, Hsu PK, Chen JY, Chou BK, Henson P, Mitani S, Xue D (November 2003). "Cell corpse engulfment mediated by C. elegans phosphatidylserine receptor through CED-5 and CED-12". Science. 302 (5650): 1563–6. doi:10.1126/science.1087641. PMID14645848.
Cui P, Qin B, Liu N, Pan G, Pei D (February 2004). "Nuclear localization of the phosphatidylserine receptor protein via multiple nuclear localization signals". Experimental Cell Research. 293 (1): 154–63. doi:10.1016/j.yexcr.2003.09.023. PMID14729065.
Cao WM, Murao K, Imachi H, Hiramine C, Abe H, Yu X, Dobashi H, Wong NC, Takahara J, Ishida T (April 2004). "Phosphatidylserine receptor cooperates with high-density lipoprotein receptor in recognition of apoptotic cells by thymic nurse cells". Journal of Molecular Endocrinology. 32 (2): 497–505. doi:10.1677/jme.0.0320497. PMID15072554.
Hong JR, Lin GH, Lin CJ, Wang WP, Lee CC, Lin TL, Wu JL (November 2004). "Phosphatidylserine receptor is required for the engulfment of dead apoptotic cells and for normal embryonic development in zebrafish". Development. 131 (21): 5417–27. doi:10.1242/dev.01409. PMID15469976.