Molecular mechanism driving disulfide formation during FGF2 oligomerization and membrane translocation (P11)

• Subject Area: Biochemistry
• Term: since 2024
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 511488495

FGF2 is an unconventionally secreted protein transported into the extracellular space by direct translocation across plasma membranes. This process involves the Na,K-ATPase and the phosphoinositide PI(4,5)P2, triggering FGF2 oligomerization and membrane pore formation. The goal of this project will be to reveal the molecular mechanism by which disulfide formation drives the production of the dimeric building blocks by which this process is initiated. A detailed understanding of this mechanism will drive the development of drugs to block the function of FGF2 in tumor-induced angiogenesis.

• DFG Programme: Collaborative Research Centres
• Subproject of: SFB 1638: Cellular membrane remodelling – how changing form creates function
• Applicant Institution: Ruprecht-Karls-Universität Heidelberg
• Project Heads: Professor Dr. Tobias Dick; Professor Dr. Walter Nickel