ADP-Ribosylation as Post-Translational Modification of Proteins: Use of Inhibitors in Cancer Control

Poltronieri, Palmiro; Misawa, Miwa; Masutani, Mitsuko

doi:10.3390/ijms221910829

Cited by 9 publications

(11 citation statements)

References 205 publications

(289 reference statements)

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“…Importantly, these hallmarks of cancer, including DNA repair deficiency, can be targeted to enhance response to various anticancer therapies ( 49 , 50 ). Indeed, PARP1 inhibitors have been used successful in the clinic for treating ovarian and breast cancers ( 3 , 32 ). Here, we outline some of the key roles of PARP10 and PARP14 in modulating DNA damage repair, and how PARP10/PARP14 status affects cancer development and the response to chemotherapeutics.…”

Section: Emerging Roles Of Mono-adp-ribosylation In Dna Repairmentioning

confidence: 99%

“…PARP1 and PARP2 are the most well studied members of this family and have been shown to be indispensable for DNA damage repair ( 3 ). They were hence highly sought-after targets for therapeutic agents and in fact PARP1 inhibitors have been used successful in the clinic for treating ovarian and breast cancers ( 3 , 32 ). As compared to PARP1 and PARP2, the other members of the PARP family are not as well studied.…”

Section: Introductionmentioning

confidence: 99%

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Mono-ADP-ribosylation by PARP10 and PARP14 in genome stability

Dhoonmoon

Nicolae

2023

NAR Cancer

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ADP-ribosylation is a post-translational modification involved in a variety of processes including DNA damage repair, transcriptional regulation, and cellular proliferation. Depending on the number of ADP moieties transferred to target proteins, ADP-ribosylation can be classified either as mono-ADP-ribosylation (MARylation) or poly-ADP-ribosylation (PARylation). This post-translational modification is catalyzed by enzymes known as ADP-ribosyltransferases (ARTs), which include the poly (ADP-ribose)-polymerase (PARP) superfamily of proteins. Certain members of the PARP family including PARP1 and PARP2 have been extensively studied and assessed as therapeutic targets. However, the other members of the PARP family of protein are not as well studied but have gained attention in recent years given findings suggesting their roles in an increasing number of cellular processes. Among these other members are PARP10 and PARP14, which have gradually emerged as key players in maintenance of genomic stability and carcinogenesis. PARP10 and PARP14 catalyze the transfer of a single ADP moiety to target proteins. Here, we summarize the current knowledge on MARylation in DNA repair and cancer, focusing on PARP10 and PARP14. We highlight the roles of PARP10 and PARP14 in cancer progression and response to chemotherapeutics and briefly discuss currently known PARP10 and PARP14 inhibitors.

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Section: Emerging Roles Of Mono-adp-ribosylation In Dna Repairmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Mono-ADP-ribosylation by PARP10 and PARP14 in genome stability

Dhoonmoon

Nicolae

2023

NAR Cancer

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“…PARP1 small-molecule inhibitors, designed as NAD + analogs, induce conformational changes in PARP1 and stabilize the complex between PARP1 and DNA, thereby "trapping" the complexes at DNA lesions. Therefore, PARP1 inhibitors have been applied as anticancer agents relying on the strategical induction of "synthetic lethality" in cancer cells carrying Breast-Cancer 1/2 (BRCA1/2) mutations [171,172]. PARP-inhibitors approved by the U.S. Food and Drug Administration (FDA), namely niraparib, olaparib, talazoparib, and rucaparib, are currently used in the therapeutic treatment of BRCA-mutated breast and ovarian cancers, as well as in tumors with dysfunctional BRCA genes [173].…”

Section: Chemical Inhibition Of Artdsmentioning

confidence: 99%

ADP-Ribosylation Post-Translational Modification: An Overview with a Focus on RNA Biology and New Pharmacological Perspectives

et al. 2022

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Cellular functions are regulated through the gene expression program by the transcription of new messenger RNAs (mRNAs), alternative RNA splicing, and protein synthesis. To this end, the post-translational modifications (PTMs) of proteins add another layer of complexity, creating a continuously fine-tuned regulatory network. ADP-ribosylation (ADPr) is an ancient reversible modification of cellular macromolecules, regulating a multitude of key functional processes as diverse as DNA damage repair (DDR), transcriptional regulation, intracellular transport, immune and stress responses, and cell survival. Additionally, due to the emerging role of ADP-ribosylation in pathological processes, ADP-ribosyltransferases (ARTs), the enzymes involved in ADPr, are attracting growing interest as new drug targets. In this review, an overview of human ARTs and their related biological functions is provided, mainly focusing on the regulation of ADP-ribosyltransferase Diphtheria toxin-like enzymes (ARTD)-dependent RNA functions. Finally, in order to unravel novel gene functional relationships, we propose the analysis of an inventory of human gene clusters, including ARTDs, which share conserved sequences at 3′ untranslated regions (UTRs).

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“…ADP ribosylation is a reversible posttranslational modification (PTM) that covalently links one or more ADP ribose unit(s) to a target protein using β -nicotinamide adenine dinucleotide ( β -NAD + ) as a donor [ 29 ]. This modification is mediated by PARP family proteins, and the target protein can be modified by a single ADP ribose unit or by a polymer chain composed of multiple ADP ribose units [ 30 ].…”

Section: Adp Ribosylation and Parp-1mentioning

confidence: 99%

PARP-1 Is a Potential Marker of Retinal Photooxidation and a Key Signal Regulator in Retinal Light Injury

Zhang

Fan

et al. 2022

Oxidative Medicine and Cellular Longevity

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Advancements in technology have resulted in increasing concerns over the safety of eye exposure to light illumination, since prolonged exposure to intensive visible light, especially to short-wavelength light in the visible spectrum, can cause photochemical damage to the retina through a photooxidation-triggered cascade reaction. Poly(ADP-ribose) polymerase-1 (PARP-1) is the ribozyme responsible for repairing DNA damage. When damage to DNA occurs, including nicks and breaks, PARP-1 is rapidly activated, synthesizing a large amount of PAR and recruiting other nuclear factors to repair the damaged DNA. However, retinal photochemical damage may lead to the overactivation of PARP-1, triggering PARP-dependent cell death, including parthanatos, necroptosis, and autophagy. In this review, we retrieved targeted articles with the keywords such as “PARP-1,” “photoreceptor,” “retinal light damage,” and “photooxidation” from databases and summarized the molecular mechanisms involved in retinal photooxidation, PARP activation, and DNA repair to clarify the key regulatory role of PARP-1 in retinal light injury and to determine whether PARP-1 may be a potential marker in response to retinal photooxidation. The highly sensitive detection of PARP-1 activity may facilitate early evaluation of the effects of light on the retina, which will provide an evidentiary basis for the future assessment of the safety of light illumination from optoelectronic products and medical devices.

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ADP-Ribosylation as Post-Translational Modification of Proteins: Use of Inhibitors in Cancer Control

Cited by 9 publications

References 205 publications

Mono-ADP-ribosylation by PARP10 and PARP14 in genome stability

Mono-ADP-ribosylation by PARP10 and PARP14 in genome stability

ADP-Ribosylation Post-Translational Modification: An Overview with a Focus on RNA Biology and New Pharmacological Perspectives

PARP-1 Is a Potential Marker of Retinal Photooxidation and a Key Signal Regulator in Retinal Light Injury

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