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Cited by 161

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

Open access
Cohen, Mickaël, Stutz, Françoise, Belgareh, Naïma, Haguenauer-Tsapis, Rosine, Dargemont, Catherine·2003·Nature Cell Biology

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.

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Metadata

Authors
Cohen, M., Stutz, F., Belgareh, N., Haguenauer-Tsapis, R., & Dargemont, C.
Venue
Nature Cell Biology
Published
2003-06-02
Volume
5
Issue
7
Pages
661-667
ISSN
  • 1465-7392 (ISSN-L)
  • 1476-4679
OpenAlex
W2061296359
Cited by
161
References
1
FWCI
3.65
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23. https://app.cochat.ai/papers/10.1038/ncb1003
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Cohen, M., Stutz, F., Belgareh, N., Haguenauer-Tsapis, R., & Dargemont, C. (2003). Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23. Nature Cell Biology. https://doi.org/10.1038/ncb1003

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