Poly(ADP-ribose)-dependent ubiquitination and its clinical implications

Christina A. Vivelo, Vinay Ayyappan, Anthony K.L. Leung

Research output: Contribution to journalReview articlepeer-review

Abstract

ADP-ribosylation—the addition of one or multiple ADP-ribose units onto proteins—is a therapeutically important post-translational modification implicated in cancer, neurodegeneration, and infectious diseases. The protein modification regulates a broad range of biological processes, including DNA repair, transcription, RNA metabolism, and the structural integrity of nonmembranous structures. The polymeric form of ADP-ribose, poly(ADP-ribose), was recently identified as a signal for triggering protein degradation through the ubiquitin-proteasome system. Using informatics analyses, we found that these ubiquitinated substrates tend to be low abundance proteins, which may serve as rate-limiting factors within signaling networks or metabolic processes. In this review, we summarize the current literature on poly(ADP-ribose)-dependent ubiquitination (PARdU) regarding its biological mechanisms, substrates, and relevance to diseases.

Original languageEnglish (US)
Pages (from-to)3-12
Number of pages10
JournalBiochemical Pharmacology
Volume167
DOIs
StatePublished - Sep 2019

Keywords

  • ADP-ribosylation
  • Poly(ADP-ribose)
  • Poly(ADP-ribose)-dependent ubiquitination
  • Protein degradation
  • Rate-limiting factors
  • Tankyrase
  • Ubiquitin-proteasome system

ASJC Scopus subject areas

  • Biochemistry
  • Pharmacology

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