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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

Academic Article
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Overview

related to degree

  • Heideker, Christine Johanna, Ph.D. in Biology, Scripps Research 2006 - 2011

authors

  • Nie, M. H.
  • Aslanian, A.
  • Prudden, J.
  • Heideker, Christine Johanna
  • Vashisht, A. A.
  • Wohlschlegel, J. A.
  • Yates III, John
  • Boddy, Michael

publication date

  • August 2012

journal

  • Journal of Biological Chemistry  Journal

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.

subject areas

  • Adenosine Triphosphatases
  • Amino Acid Motifs
  • Carrier Proteins
  • Cell Cycle Proteins
  • DNA Repair
  • DNA, Fungal
  • Genomic Instability
  • Protein Binding
  • SUMO-1 Protein
  • Schizosaccharomyces
  • Schizosaccharomyces pombe Proteins
  • Signal Transduction
  • Ubiquitin
  • Ubiquitin-Protein Ligases
  • Ubiquitination
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Identity

PubMed Central ID

  • PMC3436128

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M112.379768

PubMed ID

  • 22730331
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Additional Document Info

start page

  • 29610

end page

  • 29619

volume

  • 287

issue

  • 35

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