Structural Mechanisms and Cellular Regulation of Assembly-induced Protein Folding (B11)

• Subject Area: Biochemistry
• Term: from 2016 to 2024
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 201302640

For a major part of its proteome, cells need to regulate and control assembly processes. In our project, we investigate how conformational transitions in proteins are coupled to their assembly reactions and how these processes are supported and monitored by molecular chaperones. Our project focusses on interleukin 12 family cytokines, key regulators of human immune defence, which gain their native structure in the endoplasmic reticulum. Bridging in vitro and in vivo approaches, our findings will contribute to our understanding of how proteins acquire their native structure in a biological context. Insights gained into these processes serve as a basis to rationally engineer conformational transitions in proteins that modulate their assembly and quality control processes.

• DFG Programme: Collaborative Research Centres
• Subproject of: SFB 1035: Control of Protein Function by Conformational Switching
• Applicant Institution: Technische Universität München (TUM)
• Project Head: Professor Dr. Matthias Feige