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JMJD6

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https://www.readbyqxmd.com/read/29229759/jmjd6-induces-hotair-an-oncogenic-lincrna-by-physically-interacting-with-its-proximal-promoter
#1
Antara Biswas, Abhijith Shettar, Geetashree Mukherjee, Paturu Kondaiah, Kartiki V Desai
<span style="color: black;">Using microarray analysis we found that HOX transcript antisense intergenic RNA (HOTAIR) is upregulated by Jumonji domain containing-6 (JMJD6), a bifunctional lysyl hydroxylase and arginine demethylase. In breast cancer, JMJD6 and HOTAIR RNAs increase tumor growth and associate with poor prognosis but no molecular relationship between them is known. We show that overexpression of JMJD6 increased HOTAIR expression and JMJD6 siRNAs suppressed it in ER+ MCF-7, triple negative MDA-MB-231 and non-breast cancer HEK 293 cells...
December 11, 2017: Biochemical Journal
https://www.readbyqxmd.com/read/29187213/jmjd6-promotes-melanoma-carcinogenesis-through-regulation-of-the-alternative-splicing-of-pak1-a-key-mapk-signaling-component
#2
Xujun Liu, Wenzhe Si, Xinhua Liu, Lin He, Jie Ren, Ziran Yang, Jianguo Yang, Wanjin Li, Shumeng Liu, Fei Pei, Xiaohan Yang, Luyang Sun
BACKGROUND: Melanoma, originated from melanocytes located on the basal membrane of the epithelial tissue, is the most aggressive form of skin cancer that accounts for 75% of skin cancer-related death. Although it is believed that BRAF mutation and the mitogen-activated protein kinase (MAPK) pathway play critical roles in the pathogenesis of melanoma, how the MAPK signaling is regulated in melanoma carcinogenesis is still not fully understood. METHODS: We characterized JMJD6 expression in melanoma tissue array by immunohistochemistry analysis...
November 29, 2017: Molecular Cancer
https://www.readbyqxmd.com/read/29176719/structural-mechanism-of-the-oxygenase-jmjd6-recognition-by-the-extraterminal-et-domain-of-brd4
#3
Tsuyoshi Konuma, Di Yu, Chengcheng Zhao, Ying Ju, Rajal Sharma, Chunyan Ren, Qiang Zhang, Ming-Ming Zhou, Lei Zeng
Jumonji domain-containing protein 6 (JMJD6) is a member of the Jumonji C family of Fe(II) and 2-oxoglutarate (2OG) dependent oxygenases. It possesses unique bi-functional oxygenase activities, acting as both an arginine demethylase and a lysyl-hydroxylase. JMJD6 has been reported to be over-expressed in oral, breast, lung, and colon cancers and plays important roles in regulation of transcription through interactions with transcription regulator BRD4, histones, U2AF65, Luc7L3, and SRSF11. Here, we report a structural mechanism revealed by NMR of JMJD6 recognition by the extraterminal (ET) domain of BRD4 in that a JMJD6 peptide (Lys84-Asn96) adapts an α-helix when bound to the ET domain...
November 24, 2017: Scientific Reports
https://www.readbyqxmd.com/read/29023917/prmt1-and-jmjd6-dependent-arginine-methylation-regulate-hnf4%C3%AE-expression-and-hepatocyte-proliferation
#4
Jie Zhao, Abby Adams, Ben Roberts, Maura O'Neil, Anusha Vittal, Timothy Schmitt, Sean Kumer, Josiah Cox, Zhuan Li, Steven A Weinman, Irina Tikhanovich
Alcohol is a well-established risk factor for hepatocellular carcinoma, but the mechanisms by which it promotes liver cancer are not well understood. Several studies have shown that cellular protein arginine methylation is inhibited by alcohol. Arginine methylation is controlled by the reciprocal activity of protein arginine methyltransferases, primarily PRMT1, and a demethylase JMJD6. The aim of this study was to explore the role of arginine methylation changes in alcohol pathogenesis. We found that PRMT1 activity is inhibited in livers of mice fed with alcohol compared to pair-fed mice...
October 10, 2017: Hepatology: Official Journal of the American Association for the Study of Liver Diseases
https://www.readbyqxmd.com/read/28972166/histone-arginine-demethylase-jmjd6-is-linked-to-stress-granule-assembly-through-demethylation-of-the-stress-granule-nucleating-protein-g3bp1
#5
Wei-Chih Tsai, Lucas C Reineke, Antrix Jain, Sung Yun Jung, Richard E Lloyd
Stress granules (SG) are membrane-less organelles that are condensates of stalled translation initiation complexes and mRNAs. SG formation is a cytoprotective response to environmental stress and results from protein interactions involving regions of low amino acid complexity and poorly defined post-translational modifications of SG components. Many RNA binding proteins are methylated and we previously demonstrated that the potent SG nucleating protein G3BP1 is methylated by protein arginine methyltransferase 1 and 5 (PRMT1 and PRMT5)...
September 27, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28882645/mir-770-inhibits-tumorigenesis-and-emt-by-targeting-jmjd6-and-regulating-wnt-%C3%AE-catenin-pathway-in-non-small-cell-lung-cancer
#6
Zhiwei Zhang, Yang Yang, Xiuqiang Zhang
AIMS: MicroRNAs (miRNAs) plays important role in development and disease, especially in cancer including non-small cell lung cancer (NSCLC). However, the role of miR-770 in NSCLC remains unclear. In this study, we aimed to study the function and mechanism of miR-770 in tumorigenesis of NSCLC. MAIN METHODS: RT-qPCR was used to measure the expression levels of miR-770 in NSCLC tissues and cells. MTT assay, colony formation assay, flow cytometric analysis and transwell migration and invasion assays were performed to investigate the role of miR-770 in NSCLC cells...
November 1, 2017: Life Sciences
https://www.readbyqxmd.com/read/28793959/corrigendum-to-thymic-epithelial-cell-specific-deletion-of-jmjd6-reduces-aire-protein-expression-and-exacerbates-disease-development-in-a-mouse-model-of-autoimmune-diabetes-biochemical-and-biophysical-research-communications-489-1-2017-8-13
#7
Toyoshi Yanagihara, Takahiro Tomino, Takehito Uruno, Yoshinori Fukui
No abstract text is available yet for this article.
August 7, 2017: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/28790175/antibody-mediated-blockade-of-jmjd6-interaction-with-collagen-i-exerts-antifibrotic-and-antimetastatic-activities
#8
Silvia Miotti, Alessandro Gulino, Renata Ferri, Mariella Parenza, Agnieszka Chronowska, Daniele Lecis, Sabina Sangaletti, Elda Tagliabue, Claudio Tripodo, Mario P Colombo
JMJD6 is known to localize in the nucleus exerting histone arginine demethylase and lysyl hydroxylase activities. A novel localization of JMJD6 in the extracellular matrix, resulting from its secretion as a soluble protein, was unveiled by a new anti-JMJD6 mAb called P4E11 which was developed to identify new targets in the stroma. Recombinant JMJD6 binds with collagen type I (Coll-I), and distinct JMJD6 peptides interfere with collagen fibrillogenesis, collagen-fibronectin interaction, and adhesion of human tumor cells to the collagen substrate...
August 8, 2017: FASEB Journal: Official Publication of the Federation of American Societies for Experimental Biology
https://www.readbyqxmd.com/read/28710103/transcription-elongation-factors-are-potential-targets-in-glioblastoma
#9
(no author information available yet)
JMJD6 promotes transcription pause-release and elongation and glioblastoma cell survival in vivo.
July 14, 2017: Cancer Discovery
https://www.readbyqxmd.com/read/28678782/transcription-elongation-factors-represent-in-vivo-cancer-dependencies-in-glioblastoma
#10
Tyler E Miller, Brian B Liau, Lisa C Wallace, Andrew R Morton, Qi Xie, Deobrat Dixit, Daniel C Factor, Leo J Y Kim, James J Morrow, Qiulian Wu, Stephen C Mack, Christopher G Hubert, Shawn M Gillespie, William A Flavahan, Thomas Hoffmann, Rohit Thummalapalli, Michael T Hemann, Patrick J Paddison, Craig M Horbinski, Johannes Zuber, Peter C Scacheri, Bradley E Bernstein, Paul J Tesar, Jeremy N Rich
Glioblastoma is a universally lethal cancer with a median survival time of approximately 15 months. Despite substantial efforts to define druggable targets, there are no therapeutic options that notably extend the lifespan of patients with glioblastoma. While previous work has largely focused on in vitro cellular models, here we demonstrate a more physiologically relevant approach to target discovery in glioblastoma. We adapted pooled RNA interference (RNAi) screening technology for use in orthotopic patient-derived xenograft models, creating a high-throughput negative-selection screening platform in a functional in vivo tumour microenvironment...
July 20, 2017: Nature
https://www.readbyqxmd.com/read/28592121/inhibition-of-jmjd6-expression-reduces-the-proliferation-migration-and-invasion-of-neuroglioma-stem-cells
#11
D X Zhou, D Zhou, S Q Zhan, P Wang, K Qin, W Gan, X F Lin
Neuroglioma is the most common form of human primary malignant brain tumor, more and more studies recently showed only a small subpopulation of glioma cells which called glioma stem cells have true tumorigenic potential. Meanwhile, it was reported the overexpression of JMJD6 protein is closely involvement with the occurrence and development of multiple tumors, and JMJD6 is required for the differentiation of multiple organ, tissues and cells during embryogenesis. However, the influence of JMJD6 overexpression on neuroglioma development is unclear now...
June 8, 2017: Neoplasma
https://www.readbyqxmd.com/read/28587176/bifunctional-enzyme-jmjd6-contributes-to-multiple-disease-pathogenesis-new-twist-on-the-old-story
#12
REVIEW
Shiva Shankar Vangimalla, Murali Ganesan, Kusum K Kharbanda, Natalia A Osna
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...
June 1, 2017: Biomolecules
https://www.readbyqxmd.com/read/28546003/thymic-epithelial-cell-specific-deletion-of-jmjd6-reduces-aire-protein-expression-and-exacerbates-disease-development-in-a-mouse-model-of-autoimmune-diabetes
#13
Toyoshi Yanagihara, Takahiro Tomino, Takehito Uruno, Yoshinori Fukui
Thymic epithelial cells (TECs) establish spatially distinct microenvironments in which developing T cells are selected to mature or die. A unique property of medullary TECs is their expression of thousands of tissue-restricted self-antigens that is largely under the control of the transcriptional regulator Aire. We previously showed that Jmjd6, a lysyl hydroxylase for splicing regulatory proteins, is important for Aire protein expression and that transplantation of Jmjd6-deficient thymic stroma into athymic nude mice resulted in multiorgan autoimmunity...
July 15, 2017: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/28364140/insights-into-jumonji-c-domain-containing-protein-6-jmjd6-a-multifactorial-role-in-foot-and-mouth-disease-virus-replication-in-cells
#14
REVIEW
Paul Lawrence, Elizabeth Rieder
The Jumonji C-domain containing protein 6 (JMJD6) has had a convoluted history, and recent reports indicating a multifactorial role in foot-and-mouth disease virus (FMDV) infection have further complicated the functionality of this protein. It was first identified as the phosphatidylserine receptor on the cell surface responsible for recognizing phosphatidylserine on the surface of apoptotic cells resulting in their engulfment by phagocytic cells. Subsequent study revealed a nuclear subcellular localization, where JMJD6 participated in lysine hydroxylation and arginine demethylation of histone proteins and other non-histone proteins...
June 2017: Virus Genes
https://www.readbyqxmd.com/read/28360925/jmjd6-a-jmjc-dioxygenase-with-many-interaction-partners-and-pleiotropic-functions
#15
REVIEW
Janice Kwok, Marie O'Shea, David A Hume, Andreas Lengeling
Lysyl hydroxylation and arginyl demethylation are post-translational events that are important for many cellular processes. The jumonji domain containing protein 6 (JMJD6) has been reported to catalyze both lysyl hydroxylation and arginyl demethylation on diverse protein substrates. It also interacts directly with RNA. This review summarizes knowledge of JMJD6 functions that have emerged in the last 15 years and considers how a single Jumonji C (JmjC) domain-containing enzyme can target so many different substrates...
2017: Frontiers in Genetics
https://www.readbyqxmd.com/read/28351428/erratum-to-jmjd6-is-a-driver-of-cellular-proliferation-and-motility-and-a-marker-of-poor-prognosis-in-breast-cancer
#16
Yi Fang Lee, Lance David Miller, Xiu Bin Chan, Michael A Black, Brendan Pang, Chee Wee Ong, Manuel Salto-Tellez, Edison T Liu, Kartiki V Desai
No abstract text is available yet for this article.
March 28, 2017: Breast Cancer Research: BCR
https://www.readbyqxmd.com/read/27899633/jmjd6-and-u2af65-co-regulate-alternative-splicing-in-both-jmjd6-enzymatic-activity-dependent-and-independent-manner
#17
Jia Yi, Hai-Feng Shen, Jin-Song Qiu, Ming-Feng Huang, Wen-Juan Zhang, Jian-Cheng Ding, Xiao-Yan Zhu, Yu Zhou, Xiang-Dong Fu, Wen Liu
JMJD6, a jumonji C (Jmj C) domain-containing protein demethylase and hydroxylase, has been implicated in an array of biological processes. It has been shown that JMJD6 interacts with and hydroxylates multiple serine/arginine-rich (SR) proteins and SR related proteins, including U2AF65, all of which are known to function in alternative splicing regulation. However, whether JMJD6 is widely involved in alternative splicing and the molecular mechanism underlying JMJD6-regulated alternative splicing have remained incompletely understood...
April 7, 2017: Nucleic Acids Research
https://www.readbyqxmd.com/read/27613418/pcaf-mediated-acetylation-of-transcriptional-factor-hoxb9-suppresses-lung-adenocarcinoma-progression-by-targeting-oncogenic-protein-jmjd6
#18
Junhu Wan, Weizhi Xu, Jun Zhan, Ji Ma, Xueying Li, Yuping Xie, Jiadong Wang, Wei-Guo Zhu, Jianyuan Luo, Hongquan Zhang
HOXB9 is a homeobox domain-containing transcription factor, playing an important role in embryonic development and cancer progression. However, the precise post-translational modifications (PTMs) of HOXB9 and the corresponding roles are unclear. Here, we report that acetyltransferase p300/CBP-associated factor (PCAF) interacts with and acetylates HOXB9 both in vivo and in vitro Conversely, the acetylation of HOXB9 can be reversed by deacetylase SIRT1. Furthermore, we found that HOXB9 is acetylated at lysine 27 (AcK27)...
December 15, 2016: Nucleic Acids Research
https://www.readbyqxmd.com/read/27556302/protein-arginine-methylation-demethylation-and-cancer
#19
REVIEW
Coralie Poulard, Laura Corbo, Muriel Le Romancer
Protein arginine methylation is a common post-translational modification involved in numerous cellular processes including transcription, DNA repair, mRNA splicing and signal transduction. Currently, there are nine known members of the protein arginine methyltransferase (PRMT) family, but only one arginine demethylase has been identified, namely the Jumonji domain-containing 6 (JMJD6). Although its demethylase activity was initially challenged, its dual activity as an arginine demethylase and a lysine hydroxylase is now recognized...
October 11, 2016: Oncotarget
https://www.readbyqxmd.com/read/27171244/subsets-of-visceral-adipose-tissue-nuclei-with-distinct-levels-of-5-hydroxymethylcytosine
#20
Ping Yu, Lexiang Ji, Kevin J Lee, Miao Yu, Chuan He, Suresh Ambati, Elizabeth C McKinney, Crystal Jackson, Clifton A Baile, Robert J Schmitz, Richard B Meagher
The reprogramming of cellular memory in specific cell types, and in visceral adipocytes in particular, appears to be a fundamental aspect of obesity and its related negative health outcomes. We explored the hypothesis that adipose tissue contains epigenetically distinct subpopulations of adipocytes that are differentially potentiated to record cellular memories of their environment. Adipocytes are large, fragile, and technically difficult to efficiently isolate and fractionate. We developed fluorescence nuclear cytometry (FNC) and fluorescence activated nuclear sorting (FANS) of cellular nuclei from visceral adipose tissue (VAT) using the levels of the pan-adipocyte protein, peroxisome proliferator-activated receptor gamma-2 (PPARg2), to distinguish classes of PPARg2-Positive (PPARg2-Pos) adipocyte nuclei from PPARg2-Negative (PPARg2-Neg) leukocyte and endothelial cell nuclei...
2016: PloS One
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