The Polycomb-associated protein Rybp is a ubiquitin binding protein.
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.
Mesh Terms:
Animals, Gene Silencing, Histones, Mice, Protein Binding, Repressor Proteins, Ubiquitin, Ubiquitin-Protein Ligases, Zinc Fingers
Animals, Gene Silencing, Histones, Mice, Protein Binding, Repressor Proteins, Ubiquitin, Ubiquitin-Protein Ligases, Zinc Fingers
FEBS Lett.
Date: Nov. 13, 2006
PubMed ID: 17070805
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