title: New readers and interpretations of poly(ADP-ribosyl)ation.
abstract: Poly(ADP-ribosyl)ation (PARylation), a protein post-translational modification that was originally connected to the DNA damage response, is now known to engage in a continuously increasing number of biological processes. Despite extensive research and ceaseless, important findings about its role and mode of action, poly(ADP-ribose) remains an enigma regarding its structural complexity and diversity. The recent identification and structural characterization of four different poly(ADP-ribose) binding motifs represents a quantum leap in the comprehension of how this molecule can be decoded. Moreover, the recent discovery of a direct connection between PARylation and poly-ubiquitylation in targeting proteins for degradation by the proteasome has paved the way for a new interpretation of this protein modification. These two novel aspects, poly(ADP-ribose) recognition and readout by the ubiquitylation/proteasome system are developed here.
authors: Biotechnology and Cell Signaling, UMR7242 CNRS, Laboratory of Excellence Medalis, Université de Strasbourg, ESBS, Bd Sebastien Brant, BP 10413, 67412 Illkirch, France.
authors: Thomas
authors: T
authors: Kalisch
authors: Jean-Christophe
authors: JC
authors: Amé
authors: Françoise
authors: F
authors: Dantzer
authors: Valérie
authors: V
authors: Schreiber
mesh_terms: D000818:Animals; D004249:DNA Damage; D006801:Humans; D011064:Poly Adenosine Diphosphate Ribose / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D011485:Protein Binding; D054875:Ubiquitination
chemical_list: D011064:Poly Adenosine Diphosphate Ribose; D046988:Proteasome Endopeptidase Complex