ADP-Ribosylation of Neurofilaments by a Cytoplasmic ADP-Ribose Transferase Associated with Free mRNP

Jesser, M.; Hog, F.; Chypre, C.; Leterrier, J.F.; Mandel, P.

doi:10.1006/bbrc.1993.1908

Cited by 5 publications

(3 citation statements)

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“…Such fractions were enriched in factors that regulate translation potential and decay of mRNAs. 24,[26][27][28] Such correlation led to the hypothesis that pADPr may be involved in post-transcriptional mRNA regulation. This hypothesis was further supported by the recent discovery of two PARPs, PARP-12 and -13, that localize to the cytoplasm and contain CCCH type zinc finger RNA-binding domains.…”

Section: Multiple Cytoplasmic Parpsmentioning

confidence: 99%

Poly(ADP-ribose) regulates post-transcriptional gene regulation in the cytoplasm

et al. 2012

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Since its discovery in 1963, poly(ADP-ribose) (pADPr) has been shown to play important functions in the nucleus of multicellular eukaryotes. Each of these functions centers upon DNA metabolism, including DNA-damage repair, chromatin remodeling, transcription and telomere functions. We recently described two novel functions for pADPr in the cytoplasm, both of which involve RNA metabolism - 1) the assembly of cytoplasmic stress granules, cellular macrostructures that aggregate translationally stalled mRNA/protein complexes, and 2) modulation of microRNA activities. Multiple stress granule-localized, post-transcriptional gene regulators, including microRNA-binding argonaute family members, are substrates for pADPr modification and are increasingly modified by pADPr upon stress. Interestingly, the cytoplasmic RNA regulatory functions for PARPs are likely mediated through activities of catalytically inactive PARP-13/ARTD13/ZC3HAV1/ZAP and mono/poly(ADP-ribose)-synthesizing enzymes, including PARP-5a/ARTD5/TNKS1, PARP-12/ARTD12/ZC3HDC1 and PARP-15/ARTD7/BAL3. These data are consistent with other recent work, which suggests that mono(ADP-ribosyl)ated residues can be poly(ADP-ribosyl)ated by different enzymes.

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Section: Multiple Cytoplasmic Parpsmentioning

confidence: 99%

Poly(ADP-ribose) regulates post-transcriptional gene regulation in the cytoplasm

et al. 2012

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“…However, several previous studies suggested the existence and activation of unknown mitochondrial or cytoplasmic potentially alternatively spliced isoforms of PARP1 and PARP2 ( (194,(235)(236)(237)(238) and reviewed in (239)). In fact, data from P. Mandels group provided preliminary evidence for the existence of cytosolic and mitochondria-associated poly-ADP-ribose polymerase and poly-ADP-ribose glycohydrolase activity in primary human liver cells, rat cortical neurons and mouse fibroblasts (235)(236)(237)(238). Interestingly, PARP2 was recently suggested to be also perinuclear localized under normal physiological conditions but localized exclusively to the nucleus 6 h after irradiation at 0.5 Gy in Parp1 (+/+) MEFs cells (240).…”

Section: Activation Of An Unknown Cytoplasmic Isoform Of Parp1 or Parp2mentioning

confidence: 99%

The molecular "Jekyll and Hyde" duality of PARP1 in cell death and cell survival

Hassa¹

2009

Front Biosci

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The current literature clearly indicates that PARP1 but also PARP2 play a pivotal role in modulating the cellular responses to stress. Genetic and pharmacological studies demonstrated that overactivation of PARP1 is a key mediator of programmed-necrotic cell death in vivo. PARP1 appears to be also involved in programmed cell death processes others than necrosis, such as apoptosis or macroautophagocytotic cell death. On the other hand, growing evidence suggests that both PARP1 and PARP2 are multi-faced enzymes also playing important roles in cell survival processes. PARP1 and PARP2 were shown to be required for the maintenance of genomic integrity and to act as a survival factor for highly proliferating cells such as stem cells but also non-proliferating neuronal cells against cell death induced by oxidative stress under mild and moderate progressive damage in vivo. This review briefly summarizes the recent findings, which support a crucial role of PARP1 in different programmed cell death and cell survival processes. A special focus is placed on the proposed molecular mechanisms underlying the "Jekyll and Hyde" duality of PARP1 in cell death and cell survival pathways. A potential crosstalk between PARP1, PARP2 and other NAD+-dependent ADP-ribosyling enzymes such as Sirtuins and CD38 in cell death and survival pathways is discussed.

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“…Vimentin and desmin, constituents of the intermediate filaments , are also shown to be ADP-ribosylated by exoenzyme S of Pseudomonas aeruginosa (9) and ADPRT from chick skeletal muscle cells (10,11), respectively. Neurofilament proteins were modified by an ADPRT from cytoplasmic ribonucleoprotein particles (12). During the search of target proteins for ADP-ribosylation in the brain, we found that two cytosolic proteins, tubulin and actin, were modified by ADPRT.…”

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confidence: 96%

ADP-Ribosylation of Tubulin by Chicken NAD-Arginine ADP-Ribosyltransferase Suppresses Microtubule Formation.

Terashima¹,

Yamamori²,

Tsuchiya³

et al. 1999

Journal of Nutritional Science and Vitaminology, J Nutr Sci Vit

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SummaryWe obtained evidence that tubulin and actin, two major cytoskeletal proteins, are preferentially ADP-ribosylated in the bovine brain cytosol by NAD-arginine ADP-ribosyltransferase purified from chicken polymorphonuclear leukocytes. ADP-ribosylation of tubulin al most completely blocked self assembly of the protein. The stoichiometry of ADP-ribose incorporation into unassembled and assembled tubulin was 6 and 2mol/mol of tubulin, respectively. These findings suggest that sites of ADP-ribosylation in the unassembled tubulin molecule are crucial for tubulin assembly, and that covalently attached ADP-ribose moieties interfere with tubulin interaction by steric hindrance or conformational change. Thus, ADP-ribosylation may be involved in cytoskeletal organi zation in the brain via the modification of tubulin.

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ADP-Ribosylation of Neurofilaments by a Cytoplasmic ADP-Ribose Transferase Associated with Free mRNP

Cited by 5 publications

References 0 publications

Poly(ADP-ribose) regulates post-transcriptional gene regulation in the cytoplasm

Poly(ADP-ribose) regulates post-transcriptional gene regulation in the cytoplasm

The molecular "Jekyll and Hyde" duality of PARP1 in cell death and cell survival

ADP-Ribosylation of Tubulin by Chicken NAD-Arginine ADP-Ribosyltransferase Suppresses Microtubule Formation.

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