Institut Jacques Monod, Université Paris VII, CNRS, Bâtiment Buffon, 15 rue Hélène Brion, Paris 75205, France.
EMBO Rep. 2010 Jul;11(7):548-54. doi: 10.1038/embor.2010.74. Epub 2010 May 28.
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.
泛素依赖性过程可以被参与许多细胞功能的底物特异性去泛素化酶拮抗。在这项研究中，我们表明酵母 Ubp3-Bre5 去泛素化复合物与伴侣样 Cdc48 相互作用，Cdc48 是泛素和蛋白酶体系统的主要成分，以及 Ufd3，Cdc48 的泛素结合辅助因子。我们观察到这些伙伴对于 Ubp3-Bre5 依赖性和饥饿诱导的酵母成熟核糖体（也称为核糖体自噬）的选择性降解是必需的。相比之下，蛋白酶体依赖性降解不参与这个过程。我们的数据支持这样一种观点，即这些因素在它们的液泡降解之前合作识别和去泛素化核糖体自噬的特定底物。
