Cellular and Molecular Life Sciences CMLS

, Volume 62, Issue 7, pp 739–750

Poly-ADP-ribosylation in health and disease

Regulation of poly(ADP-ribose) metabolism by poly(ADP-ribose) glycohydrolase: where and when?
  • M.-E. Bonicalzi
  • J.-F. Haince
  • A. Droit
  • G. G. Poirier
Multi-author Review

DOI: 10.1007/s00018-004-4505-1

Cite this article as:
Bonicalzi, ME., Haince, JF., Droit, A. et al. CMLS, Cell. Mol. Life Sci. (2005) 62: 739. doi:10.1007/s00018-004-4505-1

Abstract.

Poly(ADP-ribose) glycohydrolase (PARG) is a catabolic enzyme that cleaves ADP-ribose polymers formed by members of the PARP family of enzymes. Despite its discovery and subsequent partial purification in the 1970s [1–3] and the cloning of its single gene in the late 1990s [4], little is known about the role of PARG in cell function. Because of its low abundance within cells and its extreme sensitivity to proteases, PARG has been difficult to study. The existence of several PARG isoforms with different subcellular localizations is still debated today after more than 30 years of intensive research. In this article, we want to summarize and discuss the current knowledge related to PARG, its different forms and subcellular distribution. We also examine the possible biological roles of PARG in modulating chromatin structure, transcription, DNA repair and apoptosis.

Key words.

Poly(ADP-ribose) glycohydrolase poly(ADP-ribose) polymerase poly(ADP-ribose) subcellular localization NLS NES DNA repair apoptosis 

Copyright information

© Birkhäuser Verlag, Basel 2005

Authors and Affiliations

  • M.-E. Bonicalzi
    • 1
  • J.-F. Haince
    • 1
  • A. Droit
    • 1
  • G. G. Poirier
    • 1
  1. 1.Health and Environment Unit, CHUL Research Centre Room RC-9700, Faculty of MedicineLaval UniversitySte-FoyCanada