In a longstanding cooperation with Prof. Dr. Bernd Schr?der from the Institute of Physiological Chemistry at the Technical 威尼斯赌博游戏_威尼斯赌博app-【官网】 of Dresden, the research group of Prof. Fluhreris investigating the physiological function of SPP/SPPL proteases. The collaboration particularly enables the efficient use of various model systems.

In a joint study, we were able to show that SPPL2c, a so far uncharacterized representative of the GxGDaspartyl proteases, impacts on the vesicular transport in cells and is involved in the efficient maturation of male germ cells.

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Publications

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

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Niemeyer Johannes, Mentrup Torben, Heidasch Ronny, Müller Stehphan A, Biswas Uddipta, Meyer Rieke, Papadoupoulou Alkmini A, Dederer Verena, Haug-Kr?per Martina, Adamski Vivian, Lüllmann-Rauch Renate, Bergmann Martin, Mayerhofer Artur, Saftig Paul, Wennemuth Gunther, Jessberger Rolf, Fluhrer Regina, Lichtenthaler Stefan F, Lemberg Marius K, Schr?der Bernd. The intramembrane protease SPPL2c promotes male germ cell development by cleaving phospholamban. EMBO reports 2019;20(3):e46449.

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Together with the Chair for Neuroproteomicsat the German Center for Neurodegenerative Diseases, DZNE and at the Technical 威尼斯赌博游戏_威尼斯赌博app-【官网】 of Munich, the research group of Prof. Fluhrer 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.

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Publications

Papadopoulou Alkmini A, Müller Stephan A, Mentrup Torben, Shmueli Merav D, Niemeyer Johannes, Haug-Kr?per Martina, von Blume Julia, Mayerhofer Artur, Feederle Regina, Schr?der 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-Kr?per Martina, Schr?der Bernd, Schepers Ute, Br?se 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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In collaboration with Prof. Dr. Nathan Singh at the Washington 威尼斯赌博游戏_威尼斯赌博app-【官网】 School of 威尼斯赌博游戏_威尼斯赌博app-【官网】icine, Saint Louis, we were able to show that malignant B cells with lower SPPL3 expression have an increased resistance to treatment with chimeric antigen receptor (CAR) T cells against CD19. CAR T cell therapy against CD19 is used to treat acute lymphoblastic leukemia (ALL). However, the development of resistance is a major problem. Variations in SPPL3 expression can explain the phenomenon and, thus, are the basis for further developing this therapy in the future.

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Publication

Amanda Heard, Jack H Landmann, Ava R Hansen, Alkmini Papadopolou, Yu-Sung Hsu, Mehmet Emrah Selli, John M Warrington, John Lattin, Jufang Chang, Helen Ha, Martina Haug-Kroeper, Balraj Doray, Saar Gill, Marco Ruella, Katharina E Hayer, Matthew D Weitzman, Abby M Green, Regina Fluhrer, Nathan Singh. Antigen glycosylation regulates efficacy of CAR T cells targeting CD19 Nat Commun. 2022 Jun 11;13(1):3367.

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