The role of protein O-mannosylation in ER protein quality control and cellular stress responses (11)

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

The group of Sabine Strahl (TP11) studies protein O-mannosylation which is crucial for protein surveillance in the endoplasmic reticulum. The team could pin down the Pmt1-Pmt2 mannosyltransferase complex as a central “hub” for unfolded protein O-mannosylation, and determined that Pmt1-Pmt2 activity is regulated at multiple levels in coordination with ER stress. Glycoproteomics identified O-mannosyl glycans on >20% of ER and Golgi proteins, and revealed that O-mannosylation affects the abundance/stability of 30% of the tested proteins including crucial components of the ER stress response. Now the group aims to dissect the molecular function of O-mannosyl glycosylation of key factors of the ER stress response and to investigate the operation and regulation of the Pmt1-Pmt2 complex.

• DFG Programme: Collaborative Research Centres
• Subproject of: SFB 1036: Cellular Surveillance and Damage Response
• Applicant Institution: Ruprecht-Karls-Universität Heidelberg
• Project Head: Professorin Dr. Sabine Strahl