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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23. Cohen, M., Stutz, F., Belgareh, N., Haguenauer-Tsapis, R., Dargemont, C. Nat. Cell Biol. (2003) [Pubmed]
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