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A systematic analysis of the PARP protein family identifies new functions critical for cell physiology

Author

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  • Sejal Vyas

    (Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology
    Massachusetts Institute of Technology)

  • Melissa Chesarone-Cataldo

    (Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology
    Massachusetts Institute of Technology)

  • Tanya Todorova

    (Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology
    Massachusetts Institute of Technology)

  • Yun-Han Huang

    (Massachusetts Institute of Technology)

  • Paul Chang

    (Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology
    Massachusetts Institute of Technology)

Abstract

The poly(ADP-ribose) polymerase (PARP) family of proteins use NAD+ as their substrate to modify acceptor proteins with ADP-ribose modifications. The function of most PARPs under physiological conditions is unknown. Here, to better understand this protein family, we systematically analyse the cell cycle localization of each PARP and of poly(ADP-ribose), a product of PARP activity, then identify the knockdown phenotype of each protein and perform secondary assays to elucidate function. We show that most PARPs are cytoplasmic, identify cell cycle differences in the ratio of nuclear to cytoplasmic poly(ADP-ribose) and identify four phenotypic classes of PARP function. These include the regulation of membrane structures, cell viability, cell division and the actin cytoskeleton. Further analysis of PARP14 shows that it is a component of focal adhesion complexes required for proper cell motility and focal adhesion function. In total, we show that PARP proteins are critical regulators of eukaryotic physiology.

Suggested Citation

  • Sejal Vyas & Melissa Chesarone-Cataldo & Tanya Todorova & Yun-Han Huang & Paul Chang, 2013. "A systematic analysis of the PARP protein family identifies new functions critical for cell physiology," Nature Communications, Nature, vol. 4(1), pages 1-13, October.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3240
    DOI: 10.1038/ncomms3240
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    Cited by:

    1. Matthias M. Zimmer & Anuja Kibe & Ulfert Rand & Lukas Pekarek & Liqing Ye & Stefan Buck & Redmond P. Smyth & Luka Cicin-Sain & Neva Caliskan, 2021. "The short isoform of the host antiviral protein ZAP acts as an inhibitor of SARS-CoV-2 programmed ribosomal frameshifting," Nature Communications, Nature, vol. 12(1), pages 1-15, December.
    2. Maria Di Girolamo & Gaia Fabrizio, 2018. "The ADP-Ribosyl-Transferases Diphtheria Toxin-Like (ARTDs) Family: An Overview," Challenges, MDPI, vol. 9(1), pages 1-24, May.

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