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J Biol Chem. 2003 Dec 26;278(52):51989-92. Epub 2003 Oct 30.

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

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  • 1Nucleocytoplasmic transport group, Institut Jacques Monod, Unité Mixte de Recherche 7592, CNRS, Universités Paris VI and VII, 2 Place Jussieu, Tour 43, 75251 Paris Cedex 05, France.


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.

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