Fiche publication
Date publication
septembre 2012
Auteurs
Membres identifiés du Cancéropôle Est :
Dr DANTZER Françoise
,
Dr SCHREIBER Valérie
Tous les auteurs :
Kalisch T, Ame JC, Dantzer F, Schreiber V
Lien Pubmed
Résumé
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.
Référence
Trends Biochem Sci. 2012 Sep;37(9):381-90
