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Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23

Cohen, Mickaël
Belgareh, Naïma
Haguenauer-Tsapis, Rosine
Dargemont, Catherine
Published in Nature cell biology. 2003, vol. 5, no. 7, p. 661-7
Abstract Ubiquitination is important for a broad array of cellular functions. Although reversal of this process, de-ubiquitination, most probably represents an important regulatory step contributing to cellular homeostasis, the specificity and properties of de-ubiquitination enzymes remain poorly understood. Here, we show that the Saccharomyces cerevisiae ubiquitin protease Ubp3 requires an additional protein, Bre5, to form an active de-ubiquitination complex that cleaves ubiquitin from specific substrates. In particular, this complex rescues Sec23p, a COPII subunit essential for the transport between the endoplasmic reticulum and the Golgi apparatus, from degradation by the proteasome. This probably contributes to maintaining and adapting a Sec23 expression level that is compatible with an efficient secretion pathway, and consequently with cell growth and viability.
Keywords COP-Coated Vesicles/metabolism/ultrastructureCaenorhabditis elegans ProteinsCarrier Proteins/genetics/metabolismCells, CulturedCysteine Endopeptidases/metabolism/ultrastructureEndopeptidases/deficiency/genetics/metabolismEndoplasmic Reticulum/metabolism/ultrastructureGTPase-Activating ProteinsGalactosyltransferases/deficiency/geneticsGolgi Apparatus/metabolism/ultrastructureMicroscopy, ElectronMultienzyme Complexes/metabolism/ultrastructureProteasome Endopeptidase ComplexProtein Transport/physiologySaccharomyces cerevisiae/metabolism/ultrastructureSaccharomyces cerevisiae Proteins/genetics/metabolismUbiquitin/metabolismUbiquitin Thiolesterase
PMID: 12778054
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COHEN, Mickaël et al. Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23. In: Nature Cell Biology, 2003, vol. 5, n° 7, p. 661-7. doi: 10.1038/ncb1003 https://archive-ouverte.unige.ch/unige:19438

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Deposited on : 2012-04-17

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