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Journal articles on the topic 'JmjC KDMs'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Bonnici, Joanna, Anthony Tumber, Akane Kawamura, and Christopher J. Schofield. "Inhibitors of both the N -methyl lysyl- and arginyl-demethylase activities of the JmjC oxygenases." Philosophical Transactions of the Royal Society B: Biological Sciences 373, no. 1748 (2018): 20170071. http://dx.doi.org/10.1098/rstb.2017.0071.

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The Jumonji C (JmjC) family of 2-oxoglutarate (2OG)-dependent oxygenases have established roles in the regulation of transcription via the catalysis of demethylation of N ε - methylated lysine residues in histone tails, especially the N - terminal tail of histone H3. Most human JmjC N ɛ -methyl lysine demethylases (KDMs) are complex enzymes, with ‘reader domains’ in addition to their catalytic domains. Recent biochemical evidence has shown that some, but not all, JmjC KDMs also have N ω - methyl arginyl demethylase (RDM) activity. JmjC KDM activity has been linked to multiple cancers and some

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2

Nanduri, Jayasri, Ning Wang, Benjamin L. Wang та Nanduri R. Prabhakar. "Lysine demethylase KDM6B regulates HIF-1α-mediated systemic and cellular responses to intermittent hypoxia". Physiological Genomics 53, № 9 (2021): 385–94. http://dx.doi.org/10.1152/physiolgenomics.00045.2021.

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Intermittent hypoxia (IH) is a hallmark manifestation of obstructive sleep apnea (OSA). Rodents treated with IH exhibit hypertension. Hypoxia-inducible factor (HIF)-1-dependent transcriptional activation of NADPH oxidases ( Nox) and the resulting increase in reactive oxygen species (ROS) levels is a major molecular mechanism underlying IH/OSA-induced hypertension. Jumanji C (JmjC)-containing histone lysine demethylases (JmjC-KDMs) are coactivators of HIF-1-dependent transcriptional activation. In the present study, we tested the hypothesis that JmjC-KDMs are required for IH-evoked HIF-1 transc

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3

Tarhonskaya, Hanna, Anthony Tumber, Akane Kawamura, and Christopher J. Schofield. "In Vitro Enzyme Assays for JmjC-Domain-Containing Lysine Histone Demethylases (JmjC-KDMs)." Current Protocols in Pharmacology 80, no. 1 (2018): 3.15.1–3.15.12. http://dx.doi.org/10.1002/cpph.34.

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4

Benedetti, Rosaria, Carmela Dell’Aversana, Tommaso De Marchi та ін. "Inhibition of Histone Demethylases LSD1 and UTX Regulates ERα Signaling in Breast Cancer". Cancers 11, № 12 (2019): 2027. http://dx.doi.org/10.3390/cancers11122027.

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In breast cancer, Lysine-specific demethylase-1 (LSD1) and other lysine demethylases (KDMs), such as Lysine-specific demethylase 6A also known as Ubiquitously transcribed tetratricopeptide repeat, X chromosome (UTX), are co-expressed and co-localize with estrogen receptors (ERs), suggesting the potential use of hybrid (epi)molecules to target histone methylation and therefore regulate/redirect hormone receptor signaling. Here, we report on the biological activity of a dual-KDM inhibitor (MC3324), obtained by coupling the chemical properties of tranylcypromine, a known LSD1 inhibitor, with the

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5

Konduri, Purna Chaitanya, Tianyuan Wang, Narges Salamat, and Li Zhang. "Heme, A Metabolic Sensor, Directly Regulates the Activity of the KDM4 Histone Demethylase Family and Their Interactions with Partner Proteins." Cells 9, no. 3 (2020): 773. http://dx.doi.org/10.3390/cells9030773.

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The KDM4 histone demethylase subfamily is constituted of yeast JmjC domain-containing proteins, such as Gis1, and human Gis1 orthologues, such as KDM4A/B/C. KDM4 proteins have important functions in regulating chromatin structure and gene expression in response to metabolic and nutritional stimuli. Heme acts as a versatile signaling molecule to regulate important cellular functions in diverse organisms ranging from bacteria to humans. Here, using purified KDM4 proteins containing the JmjN/C domain, we showed that heme stimulates the histone demethylase activity of the JmjN/C domains of KDM4A a

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6

He, Xinghui, Qianwen Wang, Jiao Pan, Boyu Liu, Ying Ruan, and Yong Huang. "Systematic analysis of JmjC gene family and stress-response expression of KDM5 subfamily genes in Brassica napus." PeerJ 9 (March 31, 2021): e11137. http://dx.doi.org/10.7717/peerj.11137.

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Background Jumonji C (JmjC) proteins exert critical roles in plant development and stress response through the removal of lysine methylation from histones. Brassica napus, which originated from spontaneous hybridization by Brassica rapa and Brassica oleracea, is the most important oilseed crop after soybean. In JmjC proteins of Brassica species, the structure and function and its relationship with the parents and model plant Arabidopsis thaliana remain uncharacterized. Systematic identification and analysis for JmjC family in Brassica crops can facilitate the future functional characterization

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7

Jin, Fengyan, Shaji K. Kumar, and Yun Dai. "The Lysine-Specific Demethylase KDM4A/JMJD2A Acts As a Tumor Suppressor in Multiple Myeloma." Blood 132, Supplement 1 (2018): 191. http://dx.doi.org/10.1182/blood-2018-191.

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Abstract Introduction: Histone lysine methylation, a reversible event dynamically and reciprocally regulated by lysine methyltransferases (KMTs) and demethylases (KDMs), represents one of the major epigenetic mechanisms for regulation of chromatin remodeling and gene expression re-programming. The KDM4 family, which belongs to the Jumonji C (JmjC)-domain-containing proteins (JMJDs), consists of five members, including KDM4A-E that demethylate H3K9me2/3 and/or H3K36me2/3 in a Fe2+- and α-ketoglutarate-dependent manner. KDM4 proteins are involved in various cellular processes such as gene transc

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8

Yoo, Jung, Yu Hyun Jeon, Ha Young Cho, et al. "Advances in Histone Demethylase KDM3A as a Cancer Therapeutic Target." Cancers 12, no. 5 (2020): 1098. http://dx.doi.org/10.3390/cancers12051098.

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Lysine-specific histone demethylase 3 (KDM3) subfamily proteins are H3K9me2/me1 histone demethylases that promote gene expression. The KDM3 subfamily primarily consists of four proteins (KDM3A−D). All four proteins contain the catalytic Jumonji C domain (JmjC) at their C-termini, but whether KDM3C has demethylase activity is under debate. In addition, KDM3 proteins contain a zinc-finger domain for DNA binding and an LXXLL motif for interacting with nuclear receptors. Of the KDM3 proteins, KDM3A is especially deregulated or overexpressed in multiple cancers, making it a potential cancer therape

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9

Walters, Denise K., Renee C. Tschumper, Dominique B. Hoelzinger, et al. "CRISPR-Mediated Loss of Immunoglobulin Heavy Chain in Multiple Myeloma Cell Line Results in Metabolic Pathway Alterations." Blood 132, Supplement 1 (2018): 1885. http://dx.doi.org/10.1182/blood-2018-99-114943.

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Abstract Aberrant over production of monoclonal immunoglobulin is a classic feature of the plasma cell (PC) malignancy multiple myeloma (MM). At diagnosis and more frequently upon relapse, some MM patients present with increased production of monoclonal free light chain (FLC) without a corresponding increase in intact immunoglobulin. This phenomenon is commonly referred to as light chain escape (LCE). As previously described (Walters et al. 2018, Experimental Hematology, Vol 57 p42-49), we have established a monoclonal IgA kappa MM cell line, designated as MC-B11/14, from the bone marrow (BM)

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10

Levin, May, Michal Stark, and Yehuda G. Assaraf. "The JmjN domain as a dimerization interface and a targeted inhibitor of KDM4 demethylase activity." Oncotarget 9, no. 24 (2018): 16861–82. http://dx.doi.org/10.18632/oncotarget.24717.

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11

Amendola, Pier Giorgio, Nico Zaghet, João J. Ramalho, Jens Vilstrup Johansen, Mike Boxem, and Anna Elisabetta Salcini. "JMJD-5/KDM8 regulates H3K36me2 and is required for late steps of homologous recombination and genome integrity." PLOS Genetics 13, no. 2 (2017): e1006632. http://dx.doi.org/10.1371/journal.pgen.1006632.

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12

Blanquart, Christophe, Camille Linot, Pierre-François Cartron, Daniela Tomaselli, Antonello Mai, and Philippe Bertrand. "Epigenetic Metalloenzymes." Current Medicinal Chemistry 26, no. 15 (2019): 2748–85. http://dx.doi.org/10.2174/0929867325666180706105903.

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Epigenetics controls the expression of genes and is responsible for cellular phenotypes. The fundamental basis of these mechanisms involves in part the post-translational modifications (PTMs) of DNA and proteins, in particular, the nuclear histones. DNA can be methylated or demethylated on cytosine. Histones are marked by several modifications including acetylation and/or methylation, and of particular importance are the covalent modifications of lysine. There exists a balance between addition and removal of these PTMs, leading to three groups of enzymes involved in these processes: the writer

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13

Wang, Zerong, Dongyang Liu, Baofang Xu, Ruixia Tian, and Yongchun Zuo. "Modular arrangements of sequence motifs determine the functional diversity of KDM proteins." Briefings in Bioinformatics, September 29, 2020. http://dx.doi.org/10.1093/bib/bbaa215.

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Abstract Histone lysine demethylases (KDMs) play a vital role in regulating chromatin dynamics and transcription. KDM proteins are given modular activities by its sequence motifs with obvious roles division, which endow the complex and diverse functions. In our review, according to functional features, we classify sequence motifs into four classes: catalytic motifs, targeting motifs, regulatory motifs and potential motifs. JmjC, as the main catalytic motif, combines to Fe2+ and α-ketoglutarate by residues H-D/E-H and S-N-N/Y-K-N/Y-T/S. Targeting motifs make catalytic motifs recognize specific

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14

Macedo-Silva, Catarina, Vera Miranda-Gonçalves, Ana Lameirinhas, et al. "JmjC-KDMs KDM3A and KDM6B modulate radioresistance under hypoxic conditions in esophageal squamous cell carcinoma." Cell Death & Disease 11, no. 12 (2020). http://dx.doi.org/10.1038/s41419-020-03279-y.

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AbstractEsophageal squamous cell carcinoma (ESCC), the most frequent esophageal cancer (EC) subtype, entails dismal prognosis. Hypoxia, a common feature of advanced ESCC, is involved in resistance to radiotherapy (RT). RT response in hypoxia might be modulated through epigenetic mechanisms, constituting novel targets to improve patient outcome. Post-translational methylation in histone can be partially modulated by histone lysine demethylases (KDMs), which specifically removes methyl groups in certain lysine residues. KDMs deregulation was associated with tumor aggressiveness and therapy failu

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15

Tran, Nhien, Aaron Broun, and Kai Ge. "Lysine Demethylase KDM6A in Differentiation, Development, and Cancer." Molecular and Cellular Biology 40, no. 20 (2020). http://dx.doi.org/10.1128/mcb.00341-20.

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ABSTRACT Lysine demethylase 6A (KDM6A), also known as UTX, belongs to the KDM6 family of histone H3 lysine 27 (H3K27) demethylases, which also includes UTY and KDM6B (JMJD3). The KDM6A protein contains six tetratricopeptide repeat (TPR) domains and an enzymatic Jumonji C (JmjC) domain that catalyzes the removal of di- and trimethylation on H3K27. KDM6A physically associates with histone H3 lysine 4 monomethyltransferases MLL3 (KMT2C) and MLL4 (KMT2D). Since its identification as an H3K27 demethylase in 2007, studies have reported KDM6A’s critical roles in cell differentiation, development, and

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