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

点击翻译按钮获取中文摘要

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.