Chemical genetic methodologies for identifying protein substrates of PARPs

Kelsie M. Rodriguez, Michael S. Cohen

Research output: Contribution to journalReview articlepeer-review

3 Scopus citations

Abstract

Poly-ADP-ribose-polymerases (PARPs) are a family of 17 enzymes that regulate a diverse range of cellular processes in mammalian cells. PARPs catalyze the transfer of ADP-ribose from NAD+ to target molecules, most prominently amino acids on protein substrates, in a process known as ADP-ribosylation. Identifying the direct protein substrates of individual PARP family members is an essential first step for elucidating the mechanism by which PARPs regulate a particular pathway in cells. Two distinct chemical genetic (CG) strategies have been developed for identifying the direct protein substrates of individual PARP family members. In this review, we discuss the design principles behind these two strategies and how target identification has provided novel insight into the cellular function of individual PARPs and PARP-mediated ADP-ribosylation.

Original languageEnglish (US)
Pages (from-to)390-402
Number of pages13
JournalTrends in Biochemical Sciences
Volume47
Issue number5
DOIs
StatePublished - May 2022

Keywords

  • ADP-ribosylation (ADPr)
  • MARylation
  • NAD
  • PARylation
  • chemical genetics (CG)
  • poly-ADP-ribose-polymerases (PARPs)

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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