Batool Ossareh‐Nazari1, Mélanie Bonizec1, Mickaël M. Cohen1, Svetlana Dokudovskaya1, D. François2, Christine Schaeffer‐Reiss2, Alain Van Dorsselaer2, Catherine Dargemont1
1Institut Jacques Monod, Université Paris VII, CNRS, Bâtiment Buffon 15 rue Hélène Brion Paris 75205 France
2Laboratoire de Spectrométrie de Masse Bioorganique, Institut Pluridisciplinaire Hubert Curien, Université de Strasbourg CNRS, UMR7178, 25 rue Becquerel Strasbourg 67087 France
Tóm tắt
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.
