Mechanisms governing PARP expression, localization, and activity in cells

Daniel J. Sanderson, Michael S. Cohen

Research output: Contribution to journalReview articlepeer-review

6 Scopus citations

Abstract

Poly-(ADP)-ribose polymerases (PARPs) are a family of 17 enzymes in humans that have diverse roles in cell physiology including DNA damage repair, transcription, innate immunity, and regulation of signaling pathways. The modular domain architecture of PARPs gives rise to this functional diversity. PARPs catalyze the transfer of ADP-ribose from nicotinamide adenine dinucleotide (NAD+) to targets—proteins and poly-nucleic acids. This enigmatic post-translational modification comes in two varieties: the transfer of a single unit of ADP-ribose, known as mono-ADP-ribosylation (MARylation) or the transfer of multiple units of ADP-ribose, known as poly-ADP-ribosylation (PARylation). Emerging data shows that PARPs are regulated at multiple levels to control when and where PARP-mediated M/PARylation occurs in cells. In this review, we will discuss the latest knowledge regarding the regulation of PARPs in cells: from transcription and protein stability to subcellular localization and modulation of catalytic activity.

Original languageEnglish (US)
Pages (from-to)541-554
Number of pages14
JournalCritical Reviews in Biochemistry and Molecular Biology
Volume55
Issue number6
DOIs
StatePublished - Dec 2020

Keywords

  • ADP-ribosylation
  • MARylation
  • PARylation; allosteric activation
  • Poly(ADP)-ribose polymerase
  • nicotinamide adenine dinucleotide (NAD)

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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