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Allosteric activation of the RNF146 ubiquitin ligase by a poly (ADP-ribosyl) ation signal.

Nature.. 2014-10; 
PA DaRosa, Z Wang, X Jiang, JN Pruneda, F Cong, Klevit RE, Xu W. Department of Biological Structure, University of Washington, Seattle, Washington 98195, USA.
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摘要

Protein poly(ADP-ribosyl)ation (PARylation) has a role in diverse cellular processes such as DNA repair, transcription, Wnt signalling, and cell death. Recent studies have shown that PARylation can serve as a signal for the polyubiquitination and degradation of several crucial regulatory proteins, including Axin and 3BP2 (refs 7, 8, 9). The RING-type E3 ubiquitin ligase RNF146 (also known as Iduna) is responsible for PARylation-dependent ubiquitination (PARdU). Here we provide a structural basis for RNF146-catalysed PARdU and how PARdU specificity is achieved. First, we show that iso-ADP-ribose (iso-ADPr), the smallest internal poly(ADP-ribose) (PAR) structural unit, binds between the WWE and RING domains of RN... More

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