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EMBO Rep. 2010 Jul;11(7):548-54. doi: 10.1038/embor.2010.74. Epub 2010 May 28.

Cdc48 and Ufd3, new partners of the ubiquitin protease Ubp3, are required for ribophagy.

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1
Institut Jacques Monod, Université Paris VII, CNRS, Bâtiment Buffon, 15 rue Hélène Brion, Paris 75205, France.

Abstract

Ubiquitin-dependent processes can be antagonized by substrate-specific deubiquitination enzymes involved in many cellular functions. In this study, we show that the yeast Ubp3-Bre5 deubiquitination complex interacts with both the chaperone-like Cdc48, a major actor of the ubiquitin and proteasome system, and Ufd3, a ubiquitin-binding cofactor of Cdc48. We observed that these partners are required for the Ubp3-Bre5-dependent and starvation-induced selective degradation of yeast mature ribosomes, also called ribophagy. By contrast, proteasome-dependent degradation does not participate in this process. Our data favour the idea that these factors cooperate to recognize and deubiquitinate specific substrates of ribophagy before their vacuolar degradation.

PMID:
20508643
PMCID:
PMC2897114
DOI:
10.1038/embor.2010.74
[Indexed for MEDLINE]
Free PMC Article
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