Dual recruitment of Cdc48 (p97)-Ufd1-Npl4 ubiquitin-selective segregase by small ubiquitin-like modifier protein (SUMO) and ubiquitin in SUMO-targeted ubiquitin ligase-mediated genome stability functions.
J Biol Chem
; 287(35): 29610-9, 2012 Aug 24.
Article
em En
| MEDLINE
| ID: mdl-22730331
ABSTRACT
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 a SUMO interaction 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.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Schizosaccharomyces
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Proteínas de Transporte
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Adenosina Trifosfatases
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Proteínas de Ciclo Celular
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Proteínas de Schizosaccharomyces pombe
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Proteína SUMO-1
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Ubiquitina
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Instabilidade Genômica
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Ubiquitina-Proteína Ligases
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Ubiquitinação
Idioma:
En
Ano de publicação:
2012
Tipo de documento:
Article