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FEBS Lett. 2006 Nov 13;580(26):6233-41. Epub 2006 Oct 19.

The Polycomb-associated protein Rybp is a ubiquitin binding protein.

Author information

1
Department of Molecular Genetics, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Ullmann 809 Bronx, NY 10461, USA. rachele.arrigoni@med.nyu.edu

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.

PMID:
17070805
DOI:
10.1016/j.febslet.2006.10.027
[Indexed for MEDLINE]
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