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

Date publication

juillet 2010

Auteurs

Membres identifiés du Cancéropôle Est :
Mme SCHAEFFER-REISS Christine , Dr VAN DORSSELAER Alain

Tous les auteurs :
Ossareh-Nazari B, Bonizec M, Cohen M, Dokudovskaya S, Delalande F, Schaeffer C, Van Dorsselaer A, Dargemont C

Lien Pubmed

https://www.ncbi.nlm.nih.gov/pubmed/20508643

Résumé

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.

Référence

EMBO Rep. 2010 Jul;11(7):548-54