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Trends Biochem Sci. 2012 Sep;37(9):381-90. doi: 10.1016/j.tibs.2012.06.001. Epub 2012 Jul 3.

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

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Biotechnology and Cell Signaling, UMR7242 CNRS, Laboratory of Excellence Medalis, Université de Strasbourg, ESBS, Bd Sebastien Brant, BP 10413, 67412 Illkirch, France.


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.

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