New readers and interpretations of poly(ADP-ribosyl)ation

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...

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Bibliographic Details
Published in:Trends in biochemical sciences (Amsterdam. Regular ed.) 2012-09, Vol.37 (9), p.381-390
Main Authors: Kalisch, Thomas, Amé, Jean-Christophe, Dantzer, Françoise, Schreiber, Valérie
Format: Article
Language:English
Subjects:
Animals
DNA Damage
Humans
macro domains
NAD
Poly Adenosine Diphosphate Ribose - metabolism
Poly(ADP-ribose)
post-translational modifications
Proteasome Endopeptidase Complex - metabolism
Protein Binding
Review
Ubiquitination
ubiquitylation
zinc fingers
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Summary: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.
ISSN:0968-0004
1362-4326
0968-0004
DOI:10.1016/j.tibs.2012.06.001