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

• Subject Area: Cell Biology
• Term: from 2012 to 2021
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 201348542

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.

• DFG Programme: Collaborative Research Centres
• Subproject of: SFB 1036: Cellular Surveillance and Damage Response
• Applicant Institution: Ruprecht-Karls-Universität Heidelberg
• Project Heads: Shirin Doroudgar, Ph.D.; Professor Dr. Michael Knop