1. Cell Biology
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In vivo vizualisation of Mono-ADP-ribosylation by dPARP16 upon amino-acid starvation

  1. Angelica Aguilera Gomez
  2. Marinke M van Oorschot
  3. Tineke Veenendaal
  4. Catherine Rabouille  Is a corresponding author
  1. Hubrecht Institute, Netherlands
  2. University Medical Center Utrecht, Netherlands
  3. Hubrecht Institute-KNAW, Netherlands
Research Article
  • Cited 28
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Cite this article as: eLife 2016;5:e21475 doi: 10.7554/eLife.21475

Abstract

PARP catalysed ADP-ribosylation is a post-translational modification involved in several physiological and pathological processes, including cellular stress. In order to visualise both Poly-, and Mono-, ADP-ribosylation in vivo, we engineered specific fluorescent probes. Using them, we show that amino-acid starvation triggers an unprecedented display of mono-ADP-ribosylation that governs the formation of Sec body, a recently identified stress assembly that forms in Drosophila cells. We show that dPARP16 catalytic activity is necessary and sufficient for both amino-acid starvation induced mono-ADP-ribosylation and subsequent Sec body formation and cell survival. Importantly, dPARP16 catalyses the modification of Sec16, a key Sec body component, and we show that it is a critical event for the formation of this stress assembly. Taken together our findings establish a novel example for the role of mono-ADP-ribosylation in the formation of stress assemblies, and link this modification to a metabolic stress.

Article and author information

Author details

  1. Angelica Aguilera Gomez

    Hubrecht Institute, Utrecht, Netherlands
    Competing interests
    The authors declare that no competing interests exist.
  2. Marinke M van Oorschot

    Hubrecht Institute, Utrecht, Netherlands
    Competing interests
    The authors declare that no competing interests exist.
  3. Tineke Veenendaal

    Department of Cell Biology, University Medical Center Utrecht, Utrecht, Netherlands
    Competing interests
    The authors declare that no competing interests exist.
  4. Catherine Rabouille

    Hubrecht Institute-KNAW, Utrecht, Netherlands
    For correspondence
    c.rabouille@hubrecht.eu
    Competing interests
    The authors declare that no competing interests exist.
    ORCID icon "This ORCID iD identifies the author of this article:" 0000-0002-3663-9717

Funding

Netherlands Wetenschappelijke Organisatie (822-020-016)

  • Catherine Rabouille

Hubrecht Institute

  • Catherine Rabouille

The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.

Reviewing Editor

  1. Anthony A Hyman, Max Planck Institute of Molecular Cell Biology and Genetics, Germany

Publication history

  1. Received: September 13, 2016
  2. Accepted: November 21, 2016
  3. Accepted Manuscript published: November 22, 2016 (version 1)
  4. Version of Record published: November 29, 2016 (version 2)

Copyright

© 2016, Aguilera Gomez et al.

This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.

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