Together with the Chair for Neuroproteomics at the German Center for Neurodegenerative Diseases, DZNE, and at the Technical University of Munich, the Chair for Biochemistry and Molecular Biology aims to identify new substrates for intramembrane proteases and to determine the cleavage sites within these substrates.
With help of modern mass spectrometry, we significantly expanded the range of known substrates for both the SPPL3 and the SPPL2c protease.

Papadopoulou Alkmini A, Müller Stephan A, Mentrup Torben, Shmueli Merav D, Niemeyer Johannes, Haug‐Kröper Martina, von Blume Julia, Mayerhofer Artur, Feederle Regina, Schröder Bernd, Lichtenthaler Stefan F, Fluhrer Regina. Signal peptide peptidase‐like 2c (SPPL2c) impairs vesicular transport and cleavage of SNARE proteins. EMBO reports 2019;20(3):e46451.

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Kuhn Peer-Hendrik, Voss Matthias, Haug-Kröper Martina, Schröder Bernd, Schepers Ute, Bräse Stefan, Haass Christian, Lichtenthaler Stefan F., Fluhrer Regina. Secretome analysis identifies novel signal peptide peptidase-like 3 (Sppl3) substrates and reveals a role of Sppl3 in multiple Golgi glycosylation pathways. Molecular & Cellular Proteomics 2015;14(6):1584-1598.

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Future collaborative projects will deal with the identification of new substrates for the SPPL2a and the SPPL2b protease.