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. 2006 Nov 13;580(26):6233-41.
doi: 10.1016/j.febslet.2006.10.027. Epub 2006 Oct 19.

The Polycomb-associated protein Rybp is a ubiquitin binding protein

Rachele Arrigoni  1 , Steven L Alam, Joseph A Wamstad, Vivian J Bardwell, Wesley I Sundquist, Nicole Schreiber-Agus
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Free article

The Polycomb-associated protein Rybp is a ubiquitin binding protein

Rachele Arrigoni et al. FEBS Lett. .
Free article

Erratum in

  • FEBS Lett. 2006 Dec 11;580(28-29):6754

Abstract

The Rybp protein has been promoted as a Polycomb group (PcG)-associated protein, but its molecular function has remained elusive. Here we show that Rybp is a novel ubiquitin binding protein and is itself ubiquitinated. The Rybp interacting PcG protein Ring1B, a known ubiquitin E3 ligase, promotes Rybp ubiquitination. Moreover, one target of Rybp's ubiquitin binding domain appears to be ubiquitinated histone H2A; this histone is a substrate for Ring1B's E3 ligase activity in association with gene silencing processes. These findings on Rybp provide a further link between the ubiquitination system and PcG transcriptional repressors.

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