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.

ehrmann michael-webPROTEIN QUALITY CONTROL

Prof. Dr. Michael Ehrmann

Current Positions: W3 Prof. of Microbiology, University of Duisburg-Essen;
Professorial Research Fellow, School of Biosciences, Cardiff University, UK
Group Leader: University of Konstanz, Germany
Postdoc: Harvard Medical School, Boston, MA, USA (Jon Beckwith)
PhD: University of Konstanz, Germany (Winfried Boos)

Research Interest
Mechanism and Translational Aspects of Protein Quality Control
Using the widely conserved HtrA family of serine proteases as a model, we are studying evolutionarily conserved cellular factors that are involved in key
aspects of quality control, such as detection of misfolded proteins, signal recognition and integration into the unfolded protein response pathways and regeneration of the functional state. These studies aim at revealing the general concepts governing the underlying molecular mechanisms of protein diagnosis, repair and degradation. Work on human HTRA1 showed involvements in cancer, arthritis and Alzheimer's disease.

Biochemistry, Bacterial and Mammalian Cell Biology, Molecular Genetics, Structural Biology, Chemical Biology, Analyses of patient samples

Selected Reading
Poepsel S, Sprengel A, Sacca B, Kaschani F, Kaiser M, Gatsogiannis C, Raunser S, Clausen T, Ehrmann M. Determinant of amyloid fibril degradation by the PDZ protease HTRA1. Nat Chem Biol 2015, 11, 862-9.

Mastny M, Heuck A, Kurzbauer R, Heiduk A, Boisguerin P, Volkmer R, Ehrmann M, Rodrigues CD, Rudner DZ, Clausen T. CtpB assembles a gated protease tunnel regulating cell-cell signaling during spore formation in Bacillus subtilis. Cell 2013, 155, 647–58.

Malet H, Canellas F, Sawa J, Yan J, Thalassinos K, Ehrmann M, Clausen T, Saibil HR. Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ. Nat Struct Mol Biol 2012, 19, 152-7.

Merdanovic M, Clausen T, Kaiser M, Huber R, Ehrmann M. Protein quality control in the bacterial periplasm. Annu Rev Microbiol 2011, 65, 149-68.

Clausen T, Kaiser M, Huber R, Ehrmann M. HTRA proteases: regulated proteolysis in protein quality control. Nat Rev Mol Cell Biol 2011, 12, 152-62.

Trübestein L, Tennstaedt A, Mönig T, Krojer T, Canellas F, Kaiser M, Clausen T, Ehrmann M. Substrate-induced remodeling of the active site regulates human HTRA1 activity. Nat Struct Mol Biol 2011, 18, 386-8.

Merdanovic M, Mamant N, Meltzer M, Poepsel S, Auckenthaler A, Melgaard R, Hauske P, Nagel-Steger L, Clarke AR, Kaiser M, Huber R, Ehrmann M. Determinants of structural and functional plasticity of a widely conserved protease chaperone complex. Nat Struct Mol Biol 2010, 17, 837-43.

Krojer T, Pangerl K, Kurt J, Sawa J, Stingl C, Mechtler K, Huber R, Ehrmann M, Clausen T. Interplay of PDZ and protease domain of DegP ensures efficient elimination of misfolded proteins. Nature 2008, 453, 885-90.

Ehrmann M and Clausen T. Proteolysis as a regulatory mechanism. Annu Rev Genet 2004, 38, 709-24.

Wilken C, Kitzing K, Kurzbauer R, Ehrmann M, Clausen T. Crystal structure of the DegS stress sensor: How a PDZ domain recognizes misfolded protein and activates a protease. Cell 2004, 117, 483-94 (Highlighted in 2004 Cell 117:417-9).

Krojer T, Garrido-Franco M, Huber R, Ehrmann M, Clausen T. Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine. Nature 2002, 416, 455-9 (Highlighted in 2002 Nat Rev Mol Cell Biol 3:310).

Spiess C, Beil A, Ehrmann M. A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 1999, 97, 339-47.

Read more ...