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    Nat Cell Biol. 2003 Jul;5(7):661-7.

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

    Cohen M, Stutz F, Belgareh N, Haguenauer-Tsapis R, Dargemont C.

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    Nucleocytoplasmic 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.

    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.

    PMID:
    12778054
    [PubMed - indexed for MEDLINE]

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