Aryl Hydrocarbon Receptor Activation by Dioxin Targets Phosphoenolpyruvate Carboxykinase (PEPCK) for ADP-ribosylation via 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD)-inducible Poly(ADP-ribose) Polymerase (TiPARP)

Diani-Moore, Silvia; Zhang, Sheng; Ram, Payal; Rifkind, Arleen B.

doi:10.1074/jbc.m113.458067

Cited by 27 publications

(15 citation statements)

References 67 publications

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“…Positive effects of PARP-2 on transcription are exerted through facilitating the activity of transcription (co)factors, while negative effects are due to the attraction of cofactors promoting chromatin compaction and the consequent inhibition of transcription (Szá ntó et al, 2014). PARP-7 is a cofactor for aryl-hydrocarbon receptor (Diani-Moore et al, 2013), which suggests its importance combating environmental toxins, PARP-10 interacts with c-Myc (Feijs et al, 2013), while…”

Section: Introductionmentioning

confidence: 99%

Biology of Poly(ADP-Ribose) Polymerases: The Factotums of Cell Maintenance

Bai¹

2015

Molecular Cell

394

333

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The protein family of poly(ADP-ribose) polymerases (PARPs) or diphtheria toxin-type ADP-ribose transferases (ARTDs) are multidomain proteins originally identified as DNA repair factors. There are 17 PARP enzymes in humans, and it is now evident that PARPs undertake more tasks than DNA repair. The aim of this review is to give a comprehensive view of the biological roles of the PARP family starting from the simplest biochemical reactions to complex regulatory circuits. Special attention will be laid on discussing linkage of PARP enzymes with tumor biology, oxidative stress, inflammatory, and metabolic diseases. A better understanding of PARP-mediated processes and pathologies may help in identifying new pathways and, by these, new targets to combat diseases that affect large populations and seriously shorten life expectancy and the quality of life, such as cancer, metabolic, or inflammatory diseases.

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Section: Introductionmentioning

confidence: 99%

Biology of Poly(ADP-Ribose) Polymerases: The Factotums of Cell Maintenance

Bai¹

2015

Molecular Cell

394

333

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“…Given that mitochondria are critical components of cellular metabolism, the main sites for energy production, and that many pathophysiological effects linked to TCDD exposure (e.g. diabetes, wasting syndrome, hepatic steatosis, and embryonic development) are related to metabolic pathways, researchers have focused on mitochondrial dysfunction as a potential player in TCDD-induced toxicity (Aly and Domenech, 2009; Angrish et al ., 2011; Carreira et al ., 2015; Diani-Moore et al ., 2010; Diani-Moore et al ., 2013; Forgacs et al ., 2010; Forgacs et al ., 2013). …”

Section: Introductionmentioning

confidence: 99%

Mitochondrial-targeted aryl hydrocarbon receptor and the impact of 2,3,7,8-tetrachlorodibenzo-p-dioxin on cellular respiration and the mitochondrial proteome

Hwang

Dornbos

Steidemann

et al. 2016

Toxicology and Applied Pharmacology

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The aryl hydrocarbon receptor (AHR) is a ligand-activated transcription factor within the Per-Arnt-Sim (PAS) domain superfamily. Exposure to the most potent AHR ligand, 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), is associated with various pathological effects including metabolic syndrome. While research over the last several years has demonstrated a role for oxidative stress and metabolic dysfunction in AHR-dependent TCDD-induced toxicity, the role of the mitochondria in this process has not been fully explored. Our previous research suggested that a portion of the cellular pool of AHR could be found in the mitochondria (mitoAHR). Using a protease protection assay with digitonin extraction, we have now shown that this mitoAHR is localized to the inter-membrane space (IMS) of the organelle. TCDD exposure induced a degradation of mitoAHR similar to that of cytosolic AHR. Furthermore, siRNA-mediated knockdown revealed that translocase of outer-mitochondrial membrane 20 (TOMM20) was involved in the import of AHR into the mitochondria. In addition, TCDD altered cellular respiration in an AHR-dependent manner to maintain respiratory efficiency as measured by oxygen consumption rate (OCR). Stable isotope labeling by amino acids in cell culture (SILAC) identified a battery of proteins within the mitochondrial proteome influenced by TCDD in an AHR-dependent manner. Among these, 17 proteins with |fold changes| ≥ 2 are associated with various metabolic pathways, suggesting a role of mitochondrial retrograde signaling in TCDD-mediated pathologies. Collectively, these studies suggest that mitoAHR is localized to the IMS and AHR-dependent TCDD-induced toxicity, including metabolic dysfunction, wasting syndrome, and hepatic steatosis, involves mitochondrial dysfunction.

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“…ARTD14 over-expression reproduces the TCDD effects on glucose metabolism, and it has been suggested that ARTD14 mediates these TCDD effects [178]. TCDD-dependent transcriptional induction of ARTD14 leads to ADP-ribosylation of cytosolic and mitochondrial PEPCKs [180]. However, as AHR suppression also enhances ADP-ribosylation, it is clear that the complex modulatory effects on ADP-ribosylation by AHR are far from being defined at present [180].…”

Section: Artd14mentioning

confidence: 99%

The ADP-Ribosyl-Transferases Diphtheria Toxin-Like (ARTDs) Family: An Overview

Girolamo¹,

Fabrizio²

2018

Challenges

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Poly-ADP-ribosylation is a post-translational modification that occurs in multicellular organisms, including plants and some lower unicellular eukaryotes. The founding member of the PARP family is PARP1. To date, 17 members of the PARP family have been identified, which differ from each other in terms of domain organization, transmodification targets, cellular localization, and biological functions. In recent years, considering structural and biochemical features of the different members of the PARP family, a new classification has been proposed. Thus, enzymes firstly classified as PARP are now named diphtheria-toxin-like ARTs, abbreviated to ARTDs, in accordance with the prototype bacterial toxin that their structural aspects resemble, with numbers indicating the different proteins of the family. The 17 human ARTD enzymes can be divided on the basis of their catalytic activity into polymerases (ARTD1-6), mono-ADP-ribosyl-transferases (ARTD7-17), and the inactive ARTD13. In recent years, ADP-ribosylation was intensively studied, and research was dominated by studies focusing on the role of this modification and its implication on various cellular processes. The aim of this review is to provide a general overview of the ARTD enzymes, with a special focus on mono-ARTDs.

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Aryl Hydrocarbon Receptor Activation by Dioxin Targets Phosphoenolpyruvate Carboxykinase (PEPCK) for ADP-ribosylation via 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD)-inducible Poly(ADP-ribose) Polymerase (TiPARP)

Cited by 27 publications

References 67 publications

Biology of Poly(ADP-Ribose) Polymerases: The Factotums of Cell Maintenance

Biology of Poly(ADP-Ribose) Polymerases: The Factotums of Cell Maintenance

Mitochondrial-targeted aryl hydrocarbon receptor and the impact of 2,3,7,8-tetrachlorodibenzo-p-dioxin on cellular respiration and the mitochondrial proteome

The ADP-Ribosyl-Transferases Diphtheria Toxin-Like (ARTDs) Family: An Overview

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