The Polycomb-associated protein Rybp is a ubiquitin binding protein

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

Research output: Contribution to journalArticle

46 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)6233-6241
Number of pages9
JournalFEBS Letters
Volume580
Issue number26
DOIs
StatePublished - Nov 13 2006

Keywords

  • Histone H2A
  • NZF
  • Polycomb group
  • Ring1B
  • Rybp
  • Ubiquitin

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    Arrigoni, R., Alam, S. L., Wamstad, J. A., Bardwell, V. J., Sundquist, W. I., & Schreiber-Agus, N. (2006). The Polycomb-associated protein Rybp is a ubiquitin binding protein. FEBS Letters, 580(26), 6233-6241. https://doi.org/10.1016/j.febslet.2006.10.027