Structures and Mechanisms of Enzymes Employed in the Synthesis and Degradation of PARP-Dependent Protein ADP-Ribosylation

Mol Cell. 2015 Jun 18;58(6):935-46. doi: 10.1016/j.molcel.2015.05.007.

Abstract

The poly(ADP-ribose) polymerases (PARPs) are a major family of enzymes capable of modifying proteins by ADP-ribosylation. Due to the large size and diversity of this family, PARPs affect almost every aspect of cellular life and have fundamental roles in DNA repair, transcription, heat shock and cytoplasmic stress responses, cell division, protein degradation, and much more. In the past decade, our understanding of the PARP enzymatic mechanism and activation, as well as regulation of ADP-ribosylation signals by the readers and erasers of protein ADP-ribosylation, has been significantly advanced by the emergence of new structural data, reviewed herein, which allow for better understanding of the biological roles of this widespread post-translational modification.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Catalytic Domain*
  • Glycoside Hydrolases / chemistry*
  • Glycoside Hydrolases / metabolism
  • Humans
  • Models, Molecular
  • Molecular Structure
  • Poly Adenosine Diphosphate Ribose / chemistry*
  • Poly Adenosine Diphosphate Ribose / metabolism
  • Poly(ADP-ribose) Polymerases / chemistry*
  • Poly(ADP-ribose) Polymerases / metabolism
  • Protein Binding
  • Protein Structure, Tertiary*
  • Thiolester Hydrolases / chemistry*
  • Thiolester Hydrolases / metabolism

Substances

  • Poly Adenosine Diphosphate Ribose
  • Poly(ADP-ribose) Polymerases
  • TARG1 protein, human
  • Thiolester Hydrolases
  • Glycoside Hydrolases
  • poly ADP-ribose glycohydrolase