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.
Mesh Terms:
COP-Coated Vesicles, Caenorhabditis elegans Proteins, Carrier Proteins, Cells, Cultured, Cysteine Endopeptidases, Endopeptidases, Endoplasmic Reticulum, GTPase-Activating Proteins, Galactosyltransferases, Golgi Apparatus, Microscopy, Electron, Multienzyme Complexes, Proteasome Endopeptidase Complex, Protein Transport, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Ubiquitin, Ubiquitin Thiolesterase
COP-Coated Vesicles, Caenorhabditis elegans Proteins, Carrier Proteins, Cells, Cultured, Cysteine Endopeptidases, Endopeptidases, Endoplasmic Reticulum, GTPase-Activating Proteins, Galactosyltransferases, Golgi Apparatus, Microscopy, Electron, Multienzyme Complexes, Proteasome Endopeptidase Complex, Protein Transport, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Ubiquitin, Ubiquitin Thiolesterase
Nat. Cell Biol.
Date: Jul. 01, 2003
PubMed ID: 12778054
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