Discovery of the PARP Superfamily and Focus on the Lesser Exhibited But Not Lesser Talented Members

Héberlé, Éléa; Amé, Jean‐Christophe; Illuzzi, Giuditta; Dantzer, Françoise; Schreiber, Valérie

doi:10.1007/978-3-319-14151-0_2

Cited by 4 publications

(3 citation statements)

References 156 publications

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“…We cannot exclude, however, a structural role for Parp1, Parp2, or Parp3, beyond their catalytic activity. As a PAR reader, Parp9 could also be largely compensated by other macroParps, and especially by Parp14 in mice, as Parp15 is absent in rodents . Interestingly, Parp14 regulates B‐cell functions .…”

Section: Discussionmentioning

confidence: 99%

Robust immunoglobulin class switch recombination and end joining in Parp9‐deficient mice

et al. 2017

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To mount highly specific and adapted immune responses, B lymphocytes assemble and diversify their antibody repertoire through mechanisms involving the formation of programmed DNA damage. Immunoglobulin class switch recombination (CSR) is triggered by DNA lesions induced by activation-induced cytidine deaminase, which are processed to double-stranded DNA break (DSB) intermediates. These DSBs activate the cellular DNA damage response and enroll numerous DNA repair factors, involving poly(ADP-ribose) polymerases Parp1, Parp2, and Parp3 to promote appropriate DNA repair and efficient long-range recombination. The macroParp Parp9, which is overexpressed in certain lymphomas, has been recently implicated in DSB repair, acting together with Parp1. Here, we examine the contribution of Parp9 to the resolution of physiological DSBs incurred during V(D)J recombination and CSR by generating Parp9 mice. We find that Parp9-deficient mice are viable, fertile, and do not show any overt phenotype. Moreover, we find that Parp9 is dispensable for B-cell development. Finally, we show that CSR and DNA end-joining are robust in the absence of Parp9, indicating that Parp9 is not essential in vivo to achieve physiological DSB repair, or that strong compensatory mechanisms exist.

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Section: Discussionmentioning

confidence: 99%

Robust immunoglobulin class switch recombination and end joining in Parp9‐deficient mice

et al. 2017

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“…Due to their roles in DNA repair and transcriptional control, their presence is concentrated within the nucleus. Cytoplasmic and mitochondrial PARP activity, however, have also been described (Bai, 2015;Héberlé et al, 2015;Xu et al, 2019), as is the corroborated presence of NAD +dependent ADPr in the mitochondria (Hopp et al, 2021). The recent confirmation that mitochondrial NAD + levels can influence PARP-1 nuclear activity also indicate NAD +mediated mitochondrial-nuclear crosstalk (Hopp et al, 2021).…”

Section: Parpsmentioning

confidence: 91%

NAD+ Degrading Enzymes, Evidence for Roles During Infection

Tan

Doig

2021

Front. Mol. Biosci.

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Declines in cellular nicotinamide adenine dinucleotide (NAD) contribute to metabolic dysfunction, increase susceptibility to disease, and occur as a result of pathogenic infection. The enzymatic cleavage of NAD+ transfers ADP-ribose (ADPr) to substrate proteins generating mono-ADP-ribose (MAR), poly-ADP-ribose (PAR) or O-acetyl-ADP-ribose (OAADPr). These important post-translational modifications have roles in both immune response activation and the advancement of infection. In particular, emergent data show viral infection stimulates activation of poly (ADP-ribose) polymerase (PARP) mediated NAD+ depletion and stimulates hydrolysis of existing ADP-ribosylation modifications. These studies are important for us to better understand the value of NAD+ maintenance upon the biology of infection. This review focuses specifically upon the NAD+ utilising enzymes, discusses existing knowledge surrounding their roles in infection, their NAD+ depletion capability and their influence within pathogenic infection.

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“…2). This is as important for PARP1 as it is for other PARP family members, whose emerging specialised functions [18] might depend on distinct specificities.…”

Section: Short History Of Parp Specificity Researchmentioning

confidence: 99%

Progress and outlook in studying the substrate specificities of PARPs and related enzymes

et al. 2020

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Despite decades of research on ADP-ribosyltransferases (ARTs) from the poly(ADP-ribose) polymerase (PARP) family, one key aspect of these enzymestheir substrate specificityhas remained unclear. Here, we briefly discuss the history of this area and, more extensively, the recent breakthroughs, including the identification of protein serine residues as a major substrate of PARP1 and PARP2 in human cells and of cysteine and tyrosine as potential targets of specific PARPs. On the molecular level, the modification of serine residues requires a composite active site formed by PARP1 or PARP2 together with a specificity-determining factor, HPF1; this represents a new paradigm not only for PARPs but generally for posttranslational modification (PTM) catalysis. Additionally, we discuss the identification of DNA as a substrate of PARP1, PARP2 and PARP3, and some bacterial ARTs and the discovery of noncanonical RNA capping by several PARP family members. Together, these recent findings shed new light on PARP-mediated catalysis and caution to 'expect the unexpected' when it comes to further potential substrates.

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Discovery of the PARP Superfamily and Focus on the Lesser Exhibited But Not Lesser Talented Members

Cited by 4 publications

References 156 publications

Robust immunoglobulin class switch recombination and end joining in Parp9‐deficient mice

Robust immunoglobulin class switch recombination and end joining in Parp9‐deficient mice

NAD+ Degrading Enzymes, Evidence for Roles During Infection

Progress and outlook in studying the substrate specificities of PARPs and related enzymes

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