Bernd Schröder, Technical University Dresden
SPP/SPPL-Proteases and their physiological function
In a longstanding cooperation with
Prof. Dr. Bernd Schröder from the Institute of Physiological Chemistry at the Technical University of Dresden, the Chair for Biochemistry and Molecular Biology is investigating the physiological function of SPP / SPPL proteases. The collaboration particularly enables the efficient use of various model systems.
In a recent study, we were able to show that SPPL2c, a representative of the GxGD aspartyl proteases, impacts on the vesicular transport in cells and is involved in the efficient maturation of male germ cells.
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.
Niemeyer Johannes, Mentrup Torben, Heidasch Ronny, Müller Stephan A, Biswas Uddipta, Meyer Rieke, Papadopoulou Alkmini A, Dederer Verena, Haug‐Kröper Martina, Adamski Vivian, Lüllmann‐Rauch Renate, Bergmann Martin, Mayerhofer Artur, Saftig Paul, Wennemuth Gunther, Jessberger Rolf, Fluhrer Regina, Lichtenthaler Stefan F, Lemberg Marius K, Schröder Bernd. The intramembrane protease SPPL2c promotes male germ cell development by cleaving phospholamban. EMBO reports 2019;20(3):e46449.