Defining a regulatory system at the interface of protein folding and protein degradation

折叠和降解是决定活细胞中蛋白质命运的拮抗过程。在蛋白质折叠和蛋白质降解之间必须存在谨慎的平衡，以确保细胞存活，但也有助于适应新的环境条件。这两个进程的主要参与者现已确定。分子伴侣被认为是促进蛋白质折叠的因子，而泛素/蛋白酶体系统被证明是蛋白质降解的主要途径。然而，人们对这些系统之间的相互作用知之甚少。这里描述的项目的目的是在表征的细胞通路，连接Hsc 70/Hsp 70分子伴侣机制的蛋白酶体。它应该提供的见解，在蛋白质折叠和蛋白质降解之间的接口，影响中央细胞的事件，如信号转导的调节系统。

Folding and degradation are antagonistic processes that determine the fate of a protein in the living cell. A careful balance has to exist between protein folding and protein degradation in order to ensure cell survival but also to facilitate the adaptation to new environmental conditions. Major players in both processes have now been identified. Molecular chaperones have been characterized as factors that promote protein folding, and the ubiquitin/proteasome system has been shown to represent a major pathway of protein degradation. Yet, very little is known about the regulated interplay between these systems. The project described here aims at the characterization of a cellular pathway that links the Hsc70/Hsp70 chaperone machinery to the proteasome. It should provide insights into a regulatory system at the interface between protein folding and protein degradation, affecting central cellular events such as signal transduction.