The International Max Planck Research School for Chemical and Molecular Biology (IMPRS-CMB) is a collaboration between the Max Planck Institute of Molecular Physiology and three universities, the Technical University Dortmund (TU Dortmund), the Ruhr University Bochum (RUB) and the University of Duisburg-Essen (DUE).

All four institutes are located in the Ruhr Metropolitan Area of Germany, an extremely vibrant and culturally interconnected region. The same spirit is reflected in the science of our program: research groups, with different and often complementary approaches, combine their efforts to study at the molecular level basic cell physiology.

Below you can find all the research groups that are part of IMPRS-CMB, in alphabetical order. You can also search groups by name, topic or technique.

Read about OUR SCIENCE by visiting the webpages of our Faculty Members.


Prof. Dr. Ralf Erdmann

since 2009: Chair of System Biochemistry (W3), Faculty of Medicine, RUB
2002-2009: Chair of System Biochemistry (C4), Faculty of Medicine, RUB
1998-2002: Associate Professor (C3) of Biochemistry, Free University Berlin
1995-1998: Assistant Professor (C1), RUB
1994-1995: Research Associate, Howard Hughes Medical Institute, New York
1991-1994: Rockefeller University, Lab of Günter Blobel, New York
1989-1991: Research Associate, RUB
1986-1989: PhD, Ruhr- University Bochum (RUB)

Research Interest
Peroxisomes are ubiquitous cellular organelles that are surrounded by a single membrane, multiply by division and de novo formation from the ER and play essential roles in lipid metabolism. Defects in peroxisome function of biogenesis are responsible for devastating human disorders, the mostly lethal peroxisomal diseases. Peroxisomal matrix proteins contain specific peroxisomal targeting signals (PTS1 or PTS2) that are post-translationally recognized and bound in the cytosol by the peroxisomal import receptors, which direct the receptor-cargo complex to the peroxisomal membrane. The cargo-loaded receptors insert into the peroxisomal membrane and assemble with other membrane proteins to form the translocon, which as a transient pore allows the translocation of the folded proteins across the membrane.

Research Focus
• Biogenesis and function of peroxisomes

• Structure and dynamics of the peroxisomal translocon
• Elucidation of the mechanism of the translocation of folded protein across the peroxisomal membrane
• Regulation of the function of the translocon

All common biochemical, cell biological and molecular biological techniques are established in the lab.

Selected Reading
Neuhaus A, Kooshapur H, Wolf J, Meyer NH, Madl T, Saidowsky J, Hambruch E, Lazam A, Jung M, Sattler M, Schliebs W, Erdmann R. A Novel Pex14 Protein-interacting Site of Human Pex5 Is Critical for Matrix Protein Import into Peroxisomes. J Biol Chem 2014, 289, 437-48.

Hasan S, Platta HW, Erdmann R. Import of proteins into the peroxisomal matrix. Front Physiol 2013, 4, 261.

Meinecke M, Cizmowski C, Schliebs W, Krüger V, Beck S, Wagner R, Erdmann R. The peroxisomal importomer constitutes a large and highly dynamic pore. Nat Cell Biol 2010, 12, 273-7.

Schliebs W, Girzalsky W, Erdmann R. Peroxisomal protein import and ERAD: variations on a common theme. Nat Rev Mol Cell Biol 2010, 11, 885-90.

Platta HW, El Magraoui F, Schlee D, Grunau S, Girzalsky W, Erdmann R. Ubiquitination of the peroxisomal import receptor Pex5p is required for its recycling. J Cell Biol 2007, 177, 197-204.

Platta HW, Grunau S, Rosenkranz K, Girzalsky W, Erdmann R. Functional role of the AAA peroxins in dislocation of the cycling PTS1 receptor back to the cytosol. Nat Cell Biol 2005, 8, 817-822.

Erdmann and Schliebs W. Peroxisomal matrix protein import: the transient pore model. Nat Rev Mol Cell Biol 2005, 6, 738-42.

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