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Cdc48 and Ufd3, new partners of the ubiquitin protease Ubp3, are required for ribophagy
Authors:Batool Ossareh‐Nazari  Mélanie Bonizec  Mickael Cohen  Svetlana Dokudovskaya  François Delalande  Christine Schaeffer  Alain Van Dorsselaer  Catherine Dargemont
Institution:1. Institut Jacques Monod, Université Paris VII, CNRS, Batiment Buffon, 15 rue Hélène Brion, Paris, 75205 France;2. Laboratoire de Spectrométrie de Masse Bioorganique, Institut Pluridisciplinaire Hubert Curien, Université de Strasbourg, CNRS, UMR7178, 25 rue Becquerel, Strasbourg, 67087 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.
Keywords:ubiquitin  deubiquitination  proteasome  ribophagy
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