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

Cohen, Mickaël
Dargemont, Catherine
Published in Journal of Biological Chemistry. 2003, vol. 278, no. 52, p. 51989-92
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.
Keywords Amino Acid SequenceBiological TransportCOP-Coated VesiclesEndopeptidases/metabolismEndoplasmic Reticulum/metabolism/physiologyGTPase-Activating ProteinsGlutathione Transferase/metabolismGolgi Apparatus/physiologyMolecular Sequence DataProtein BindingSaccharomyces cerevisiae/physiologySaccharomyces cerevisiae Proteins/metabolismSequence Homology, Amino AcidSignal TransductionTemperatureTwo-Hybrid System TechniquesUbiquitin/metabolismUbiquitin Thiolesterase
PMID: 14593109
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COHEN, Mickaël, STUTZ, Françoise, DARGEMONT, Catherine. Deubiquitination, a new player in Golgi to endoplasmic reticulum retrograde transport. In: Journal of Biological Chemistry, 2003, vol. 278, n° 52, p. 51989-92. doi: 10.1074/jbc.C300451200 https://archive-ouverte.unige.ch/unige:19436

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Deposited on : 2012-04-17

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