Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 287, Issue 35, Pages 29610-29619Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M112.379768
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Funding
- National Institutes of Health [GM068608, GM081840, GM093600, P41 RR011823]
- Leukemia and Lymphoma Society
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Protein modification by SUMO and ubiquitin critically impacts genome stability via effectors that read their signals using SUMO interaction motifs or ubiquitin binding domains, respectively. A novel mixed SUMO and ubiquitin signal is generated by the SUMO-targeted ubiquitin ligase (STUbL), which ubiquitylates SUMO conjugates. Herein, we determine that the ubiquitin-selective segregase Cdc48-Ufd1-Npl4 also binds SUMO via aSUMOinteraction motif in Ufd1 and can thus act as a selective receptor for STUbL targets. Indeed, we define key cooperative DNA repair functions for Cdc48-Ufd1-Npl4 and STUbL, thereby revealing a new signaling mechanism involving dual recruitment by SUMO and ubiquitin for Cdc48-Ufd1-Npl4 functions in maintaining genome stability.
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