The emerging roles of ribosomal histidyl hydroxylases in cell biology, physiology and disease

Bundred, James; Hendrix, Eline; Coleman, Mathew L.

doi:10.1007/s00018-018-2903-z

Cited by 20 publications

(38 citation statements)

References 82 publications

(178 reference statements)

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“…A similar investigation into published JMJD6 substrates was also unable to confirm other proposed targets and biochemical activities beyond lysyl hydroxylation [123], including a reported histone arginyl demethylase activity [124]. In fact, initial assignments of histone demethylase activity (or declaration of KDM activity even in the absence of evidence), is a theme among the JmjC-only sub-family of 2OG-oxygenases (as discussed in [16,17,111]) (e.g. MINA, NO66, JMJD4, and JMJD7).…”

Section: Activity Assignment Controversymentioning

confidence: 94%

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Human 2-oxoglutarate-dependent oxygenases: nutrient sensors, stress responders, and disease mediators

Fletcher

Coleman

2020

Biochemical Society Transactions

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Fe(II)/2-oxoglutarate (2OG)-dependent oxygenases are a conserved enzyme class that catalyse diverse oxidative reactions across nature. In humans, these enzymes hydroxylate a broad range of biological substrates including DNA, RNA, proteins and some metabolic intermediates. Correspondingly, members of the 2OG-dependent oxygenase superfamily have been linked to fundamental biological processes, and found dysregulated in numerous human diseases. Such findings have stimulated efforts to understand both the biochemical activities and cellular functions of these enzymes, as many have been poorly studied. In this review, we focus on human 2OG-dependent oxygenases catalysing the hydroxylation of protein and polynucleotide substrates. We discuss their modulation by changes in the cellular microenvironment, particularly with respect to oxygen, iron, 2OG and the effects of oncometabolites. We also describe emerging evidence that these enzymes are responsive to cellular stresses including hypoxia and DNA damage. Moreover, we examine how dysregulation of 2OG-dependent oxygenases is associated with human disease, and the apparent paradoxical role for some of these enzymes during cancer development. Finally, we discuss some of the challenges associated with assigning biochemical activities and cellular functions to 2OG-dependent oxygenases.

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Section: Activity Assignment Controversymentioning

confidence: 94%

“…In fact, TET2 is one of the most commonly mutated genes in AML [110]. For other 2OG-oxygenases however, particularly those in the JmjC-only sub-family, the picture is less clear [17,111]. In the case of arginyl hydroxylase JMJD5, for example, multiple studies have described both pro-and antitumourigenic functions.…”

Section: Og-oxygenases: Disease Mediatorsmentioning

confidence: 99%

Human 2-oxoglutarate-dependent oxygenases: nutrient sensors, stress responders, and disease mediators

Fletcher

Coleman

2020

Biochemical Society Transactions

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“…The involvement of the JMJD-type demethylases in human physiology and diseases has been well documented, for instance, in the development, metabolic diseases, inflammation, and various types of cancer [3,4]. JMJD10/MINA53 belongs to a phylogenetically distinct group, known as the "JmjC-only" 2-oxoglutarate (2OG)-oxygenase subfamily, as it has a JmjC domain, which is capable of catalyzing protein hydroxylation (and demethylation via hydroxylation reaction) in a 2OG-dependent oxygenase manner and has no other immediate functional domains [5]. An investigation of biochemical activity revealed that JMJD10 has hydroxylation activity toward Rpl27a [6].…”

Section: Introductionmentioning

confidence: 99%

“…Several reports suggest the overexpression of JMJD10/MINA53 in multiple cancers such as colorectal, lung, esophageal, glioblastoma, lymphoma, cholangiocarcinoma, gingival squamous cell carcinoma, neuroblastoma, liver, pancreatic, multiple myeloma, breast, and gastric cancer [5,10,[18][19][20][21][22][23][24][25][26]. An intricate role has also been described for JMJD10/MINA53, as overexpression may not always correlate with poor patient prognosis [5]. Supposedly, JMJD10/MINA53 might have opposing roles at different stages of tumorigenesis as it exhibits a growth-promoting role in early cancer but a tumor suppressor role in the later stages of the disease [5].…”

Section: Introductionmentioning

confidence: 99%

“…An intricate role has also been described for JMJD10/MINA53, as overexpression may not always correlate with poor patient prognosis [5]. Supposedly, JMJD10/MINA53 might have opposing roles at different stages of tumorigenesis as it exhibits a growth-promoting role in early cancer but a tumor suppressor role in the later stages of the disease [5]. Hence, the molecular signatures and mechanisms of JMJD10/MINA53 in cancer largely remain to be elucidated, in particular, the molecular signatures in gastric cancer.…”

Section: Introductionmentioning

confidence: 99%

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Molecular Signatures of JMJD10/MINA53 in Gastric Cancer

Aziz

Hong

et al. 2020

Cancers

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The JMJD10 gene and its encoded protein MYC-induced nuclear antigen (MINA53) are associated with multiple cancers. Besides having both an oncogenic and tumor suppressor function, the intricate role of JMJD10 in cancer is complex as it depends on the cancer type. In particular, the functional role of JMJD10/MINA53 in gastric cancer has been poorly understood. In this study, we have unraveled the molecular signatures and functional roles of JMJD10/MINA53 in gastric cancer by multiple approaches, i.e., multi-omics bioinformatics study, analysis of human gastric cancer tissues, and studies in vitro using knockdown or overexpression strategies in gastric cancer cell lines. The results indicated that the JMJD10 gene and MINA53 protein are commonly overexpressed in cancer patients. JMJD10/MINA53 is involved in the regulation of proliferation and survival of gastric cancer by controlling cell cycle gene expression. These processes are highly associated with MINA53 enzymatic activity in the regulation of H3K9me3 methylation status and controlling activation of AP-1 signaling pathways. This highlights the oncogenic role of JMJD10/MINA53 in gastric cancer and opens the opportunity to develop therapeutic targeting of JMJD10/MINA53 in gastric cancer.

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Promiscuous Enzymes for Residue‐Specific Peptide and Protein Late‐Stage Functionalization

Alexander

Elshahawi

2023

ChemBioChem

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The late‐stage functionalization of peptides and proteins holds significant promise for drug discovery and facilitates bioorthogonal chemistry. This selective functionalization leads to innovative advances in in vitro and in vivo biological research. However, it is a challenging endeavor to selectively target a certain amino acid or position in the presence of other residues containing reactive groups. Biocatalysis has emerged as a powerful tool for selective, efficient, and economical modifications of molecules. Enzymes that have the ability to modify multiple complex substrates or selectively install nonnative handles have wide applications. Herein, we highlight enzymes with broad substrate tolerance that have been demonstrated to modify a specific amino acid residue in simple or complex peptides and/or proteins at late‐stage. The different substrates accepted by these enzymes are mentioned together with the reported downstream bioorthogonal reactions that have benefited from the enzymatic selective modifications.

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The emerging roles of ribosomal histidyl hydroxylases in cell biology, physiology and disease

Cited by 20 publications

References 82 publications

Human 2-oxoglutarate-dependent oxygenases: nutrient sensors, stress responders, and disease mediators

Human 2-oxoglutarate-dependent oxygenases: nutrient sensors, stress responders, and disease mediators

Molecular Signatures of JMJD10/MINA53 in Gastric Cancer

Promiscuous Enzymes for Residue‐Specific Peptide and Protein Late‐Stage Functionalization

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