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Article
Subject Categories: Signal Transduction | Genome Stability & Dynamics
The EMBO Journal (2007) 26, 4102–4112, doi:10.1038/sj.emboj.7601839
Published online 30 August 2007
Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins
Huaiyu Sun, Joel D Leverson1 and Tony Hunter
Molecular and Cell Biology Laboratory, Salk Institute for Biological Studies, La Jolla, CA, USA

To whom correspondence should be addressed
Tony Hunter, Molecular and Cell Biology Laboratory, Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, CA 92037, USA. Tel.: +1 858 453 4100 ext 1385; Fax: +1 858 457 4765; E-mail: hunter@salk.edu

1 Present address: Abbott Laboratories, Global Pharmaceutical Research Division, Cancer Division, 100 Abbott Park Road, Abbott Park, IL 60064, USA

Received 11 May 2007; Accepted 2 August 2007; Published online 30 August 2007.
Abstract
The function of small ubiquitin-like modifier (SUMO)-binding proteins is key to understanding how SUMOylation regulates cellular processes. We identified two related Schizosaccharomyces pombe proteins, Rfp1 and Rfp2, each having an N-terminal SUMO-interacting motif (SIM) and a C-terminal RING-finger domain. Genetic analysis shows that Rfp1 and Rfp2 have redundant functions; together, they are essential for cell growth and genome stability. Mammalian RNF4, an active ubiquitin E3 ligase, is an orthologue of Rfp1/Rfp2. Rfp1 and Rfp2 lack E3 activity but recruit Slx8, an active RING-finger ubiquitin ligase, through a RING–RING interaction, to form a functional E3. RNF4 complements the growth and genomic stability defects of rfp1rfp2, slx8, and rfp1rfp2slx8 mutant cells. Both the Rfp-Slx8 complex and RNF4 specifically ubiquitylate artificial SUMO-containing substrates in vitro in a SUMO binding-dependent manner. SUMOylated proteins accumulate in rfp1rfp2 double-null cells, suggesting that Rfp/Slx8 proteins may promote ubiquitin-dependent degradation of SUMOylated targets. Hence, we describe a family of SIM-containing RING-finger proteins that potentially regulates eukaryotic genome stability through linking SUMO-interaction with ubiquitin conjugation.
Keywords: SUMO, SUMO-interacting motif, ubiquitin, RING, E3 ligase
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