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

Leung, Anthony K.L.; Todorova, Tanya; Ando, Yoshinari; Chang, Paul

doi:10.4161/rna.19899

Cited by 59 publications

(55 citation statements)

References 55 publications

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“…Both PARP9 (23) and PARP13 (14,19,21) lack automodification activity. Based on these findings, they have been suggested to lack ADP-ribosyltransferase activity altogether (21,24). However, robust assessment of PARP enzymatic activity is complicated by the fact that the physiological target proteins, putative activators, and minimal domain compositions required for activity are unknown for most family members.…”

Section: The Mammalian Poly(adp-ribose) Polymerase (Parp) Family Inclmentioning

confidence: 99%

Structural Basis for Lack of ADP-ribosyltransferase Activity in Poly(ADP-ribose) Polymerase-13/Zinc Finger Antiviral Protein

Karlberg

Klepsch

Thorsell

et al. 2015

Journal of Biological Chemistry

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Section: The Mammalian Poly(adp-ribose) Polymerase (Parp) Family Inclmentioning

confidence: 99%

Structural Basis for Lack of ADP-ribosyltransferase Activity in Poly(ADP-ribose) Polymerase-13/Zinc Finger Antiviral Protein

Karlberg

Klepsch

Thorsell

et al. 2015

Journal of Biological Chemistry

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“…Certain RBDs tend to bind short sequences and display poor affinity for RNA; however, the interaction interface formed by multiple modules ensures a high affinity and specificity towards an RNA target. The superposition of weak interactions facilitates the regulation of assembly and disassembly of RNP complexes that may be mediated by an RNA-like polymer of poly(ADP-ribose) [76, 77]. Owing to the modular structure of RNA-binding proteins, different RNAs may be targeted by the same RBP [75].…”

Section: Rna-binding Proteins: Module Organizationmentioning

confidence: 99%

At the Interface of Three Nucleic Acids: The Role of RNA-Binding Proteins and Poly(ADP-ribose) in DNA Repair

Alemasova

Lavrik

2017

Acta Naturae

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RNA-binding proteins (RBPs) regulate RNA metabolism, from synthesis to decay. When bound to RNA, RBPs act as guardians of the genome integrity at different levels, from DNA damage prevention to the post-transcriptional regulation of gene expression. Recently, RBPs have been shown to participate in DNA repair. This fact is of special interest as DNA repair pathways do not generally involve RNA. DNA damage in higher organisms triggers the formation of the RNA-like polymer – poly(ADP-ribose) (PAR). Nucleic acid-like properties allow PAR to recruit DNA- and RNA-binding proteins to the site of DNA damage. It is suggested that poly(ADP-ribose) and RBPs not only modulate the activities of DNA repair factors, but that they also play an important role in the formation of transient repairosome complexes in the nucleus. Cytoplasmic biomolecules are subjected to similar sorting during the formation of RNA assemblages by functionally related mRNAs and promiscuous RBPs. The Y-box-binding protein 1 (YB-1) is the major component of cytoplasmic RNA granules. Although YB-1 is a classic RNA-binding protein, it is now regarded as a non-canonical factor of DNA repair.

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“…This thus led to further investigation of the nature of these cell bodies. Previous studies demonstrated that, differently from ARTD10, other ARTD enzymes, including ARTD5, ARTD7, ARTD12, ARTD13, localise into stress granules and induce stress granules formation when overexpressed in cells [47,48], suggesting that ADP-ribosylation can favor ARTDs recruitment into these distinct proteins aggregates. We thus analysed whether ARTD10-CD can be recruited into stress granules.…”

Section: The Catalytic Domain Of Artd10 Sequesters Gapdh Into Stressmentioning

confidence: 99%

ARTD10/PARP10 Induces ADP-Ribosylation of GAPDH and Recruits GAPDH into Cytosolic Membrane-Free Cell Bodies When Overexpressed in Mammalian Cells

et al. 2018

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Protein ADP-ribosylation is a reversible post-translational modification of cellular proteins that is catalysed by enzymes that transfer one (mono) or several (poly) units of ADP-ribose from β-NAD + to a specific amino acid of the target protein. The most studied member of the ADP-ribosyltransferase family is PARP1 (also known as ADP-ribosyltransferase diphtheria toxin-like 1, ARTD1), which is directly activated by DNA strand breaks and is involved in DNA damage repair, chromatin remodelling and transcriptional regulation. Much less is known about the further 16 members of this family. Among these, ARTD10/PARP10 has been previously characterised as a mono-ADP-ribosyltransferase with a role in cell proliferation and in NF-kB signalling. In the present study, we identified the glycolytic enzyme GAPDH as an interactor and a novel cellular target for ARTD10/PARP10. Moreover, we detected the co-localisation of GAPDH and ARTD10/PARP10 in well-defined cytosolic bodies, which we show here to be membrane-free, rounded structures using immunogold labelling and electron microscopy. Using the cognitive binding module macro domain to visualise ADP-ribosylated proteins by immunofluorescence microscopy in cells over-expressing the ARTD10/PARP10 enzyme, we show that the staining of the ARTD10/PARP10-dependent cytosolic bodies was lost when the cells were treated with compounds that inhibit ARTD10/PARP10, either by directly inhibiting the enzyme or by reducing the cellular NAD + levels. In parallel, the same treatment affected the co-localisation of GAPDH and ARTD10/PARP10, as GAPDH disappeared from the cytosolic cell bodies, which indicates that its presence there depends on the catalytic activity of ARTD10/PARP10. In line with this, in cells over-expressing the ARTD10/PARP10 catalytic domain alone, which we show here to form stress granules, GAPDH was recruited into stress granules. These data identify ARTD10/PARP10 as the enzyme that modifies and recruits GAPDH into cytosolic structures.

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

Cited by 59 publications

References 55 publications

Structural Basis for Lack of ADP-ribosyltransferase Activity in Poly(ADP-ribose) Polymerase-13/Zinc Finger Antiviral Protein

Structural Basis for Lack of ADP-ribosyltransferase Activity in Poly(ADP-ribose) Polymerase-13/Zinc Finger Antiviral Protein

At the Interface of Three Nucleic Acids: The Role of RNA-Binding Proteins and Poly(ADP-ribose) in DNA Repair

ARTD10/PARP10 Induces ADP-Ribosylation of GAPDH and Recruits GAPDH into Cytosolic Membrane-Free Cell Bodies When Overexpressed in Mammalian Cells

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