Brief career history
- 2012-present: Senior Lecturer, Department of Biomedical Science, The University of Sheffield
- 2006-2012: Privatdozent, Group leader, Ruhr-University Bochum, Germany
- 2005-2006: Research Associate, Yale University School of Medicine, USA
- 2003-2005: Feodor Lynen Fellow (Alexander von Humboldt foundation), Yale University School of Medicine, USA
- 1998-2003: Junior group leader, Ruhr-University Bochum, Germany
- 1996-1998: Postdoctoral work, Ruhr-University Bochum, Germany
- 1993-1996: PhD, Ruhr-University Bochum, Germany
- 1987-1992: Diploma, Ruhr-University Bochum, Germany
Membrane trafficking and signalling in polarised cells. Role of multi-PDZ domain proteins in cancer formation, metastasis and tumor invasion
Our group is interested in the regulation of membrane trafficking and its relation to human diseases. In particular we are interested in the molecular mechanism leading to Lowe syndrome, a X-linked disease characterized by congenital cataracts, mental retardation and kidney failure. Moreover, we analyze the molecular function of multi-PDZ domain proteins (PTPN13 and FRMPD2) in vesicular trafficking and signal transduction as well as their role in cancer development and progression.
- Coordinator of the Marie Curie Initial Training Network (ITN) TRANSPOL
- Visiting scientist Yale University School of Medicine (Sept/Oct. 2011)
- Eurotrans-Bio (ETB) Award (2011) (consortium)
- Feodor Lynen postdoctoral fellow (Alexander von Humboldt foundation) (2003-2005)
|EU Marie Curie-CIG-project Endosignal
Inflammatory bowel disease is a devastating disease affecting several million people in Europe. This project addresses the molecular mechanism of inflammatory bowel disease. The multi-PDZ domain protein FRMPD2 (FERM and PDZ domain containing protein 2) has been shown to be an integral part of the immune host defense of epithelial cells by recruiting NOD2 (Nucleotide-binding and oligomerization protein 2), a key player of the innate immune system, to the basolateral membrane in epithelial cells.
In addition, FRMPD2 is involved in epithelial cell/cell adhesion regulating tight junction formation. Interaction of NOD2 with FRMPD2 places the NOD2 protein into a novel context being part of a larger protein complex. Using an interdisciplinary approach combining state of the art techniques from cell biology, protein chemistry, membrane physics and developmental genetics, this project aims at the identification and functional characterization of novel components of the FRMPD2 protein complex.
In particular, this protein complex will be characterized with respect to mechanisms relevant to epithelial cell polarization and inflammatory bowel disease. Finally, the project aims to complement in vitro mechanistic and cell culture data with in vivo results by analyzing the role of the FRMPD2 complex in zebrafish development. The results of this project will lead to a better molecular understanding of the disease opening potentially new avenues of treatments.
Full publications list
Biochemical and mechanochemical mechanisms of epithelial cell polarisation
Cell polarity is at the crossroads of differentiation and growth, and loss of cell polarity is a hallmark of cancer and other relevant diseases. Our group is interested in the regulation of cell polarization and its relation to human diseases. In particular, we analyze the molecular function of multi-PDZ domain proteins (PTPN13/PTP-BL and FRMPD2) in epithelial cell polarization as well as their role in cancer development and progression. PTPN13 and FRMPD2 are closely related and represent members of a small family of peripheral membrane proteins containing multiple PDZ domains as well as a FERM domain.
Both proteins are strongly expressed in epithelial cells. PTPN13 assembles an apical protein complex, whereas FRMPD2 organizes a protein complex at the basolateral membrane in epithelial cells. PTPN13 is involved in carcinogenesis and mediates resistance to Fas induced apoptosis by an unknown mechanism. FRMPD2 has recently been identified by our group and plays a role in cell/cell adhesion regulation. We are identifying PTPN13- and FRMPD2- protein complexes and based on this suggesting a potential role in intracellular membrane trafficking and cell adhesion for both proteins.
We analyze corresponding molecular mechanisms of cell polarization in 2D and 3D epithelial cell culture systems and have recently introduced chip-based micropatterning to control cell polarization by mechanical means. In addition, we analyze our target proteins in vivo using zebra fish as a model system.
Lab phone extension is: 22364
- Jochen Guck Technical University, Dresden, Germany