Applying quantitative profiling and imaging methods to explore the proteolytic plasticity of protein N-termini and protein misfolding processest (10)

Knop/Doroudgar （TP10）将采用质谱方法和N-degron稳定性分析来探索蛋白质n端在典型和非典型氨基肽酶的n端乙酰化和蛋白质水解过程中的可塑性。通过筛选，他们将把n端可塑性与全长蛋白的生理功能和蛋白质质量和稳态中的作用联系起来。在Doroudgar子项目中，他们将采用蛋白质稳态和肌节相关蛋白周转的动态成像来了解其稳态调节以及蛋白质错误折叠和聚集如何影响心肌细胞收缩功能。

Knop/Doroudgar (TP10) will employ mass spec approaches and N-degron stability profiling to explore the plasticity of N-termini of proteins with respect to N-terminal acetylation and proteolytic processing by canonical and non-canonical aminopeptidases. Using screening they will then link N-terminal plasticity to physiological functions and roles in protein quality and homeostasis of the full-length proteins. In the Doroudgar sub-project they will employ dynamic imaging of protein homeostasis and turnover of sarcomere associated proteins to understand their homeostasis regulation and how protein misfolding and aggregation affects cardiac myocyte contractile functions.