| First Author | Arrigoni R | Year | 2006 |
| Journal | FEBS Lett | Volume | 580 |
| Issue | 26 | Pages | 6233-41 |
| PubMed ID | 17070805 | Mgi Jnum | J:117714 |
| Mgi Id | MGI:3697286 | Doi | 10.1016/j.febslet.2006.10.027 |
| Citation | Arrigoni R, et al. (2006) The Polycomb-associated protein Rybp is a ubiquitin binding protein. FEBS Lett 580(26):6233-41 |
| abstractText | 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. |
