Deubiquitination, a new player in Golgi to endoplasmic reticulum retrograde transport

J Biol Chem. 2003 Dec 26;278(52):51989-92. doi: 10.1074/jbc.C300451200. Epub 2003 Oct 30.

Abstract

Modification by ubiquitin plays a major role in a broad array of cellular functions. Although reversal of this process, deubiquitination, likely represents an important regulatory step contributing to cellular homeostasis, functions of deubiquitination enzymes still remain poorly characterized. We have previously shown that the ubiquitin protease Ubp3p requires a co-factor, Bre5p, to specifically deubiquitinate the coat protein complex II (COPII) subunit Sec23p, which is involved in anterograde transport between endoplasmic reticulum and Golgi compartments. In the present report, we show that disruption of BRE5 gene also led to a defect in the retrograde transport from the Golgi to the endoplasmic reticulum. Further analysis indicate that the COPI subunit beta'-COP represents another substrate of the Ubp3p.Bre5p complex. All together, our results indicate that the Ubp3p.Bre5p deubiquitination complex co-regulates anterograde and retrograde transports between endoplasmic reticulum and Golgi compartments.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Biological Transport
  • COP-Coated Vesicles
  • Endopeptidases / metabolism
  • Endoplasmic Reticulum / metabolism
  • Endoplasmic Reticulum / physiology*
  • GTPase-Activating Proteins
  • Glutathione Transferase / metabolism
  • Golgi Apparatus / physiology*
  • Molecular Sequence Data
  • Protein Binding
  • Saccharomyces cerevisiae / physiology*
  • Saccharomyces cerevisiae Proteins / metabolism
  • Sequence Homology, Amino Acid
  • Signal Transduction
  • Temperature
  • Two-Hybrid System Techniques
  • Ubiquitin / metabolism*
  • Ubiquitin Thiolesterase

Substances

  • GTPase-Activating Proteins
  • SEC23 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • USP10 protein, human
  • Ubiquitin
  • Glutathione Transferase
  • Endopeptidases
  • Ubiquitin Thiolesterase
  • UBP3 protein, S cerevisiae
  • ubiquitin-Nalpha-protein hydrolase