• sense clinically
  • think mechanistically
  • act interdisciplinarily
  • treat innovatively

Prof. Dr. rer. nat. Petra Knaus

Knaus Group - Signal Transduction
Institute of Chemistry and Biochemistry
Freie Universität Berlin
Thielallee 63
Room 208
14195 Berlin
Tel: +49 40 838 52938 (Secretary)

E-Mail: knaus(at)zedat.fu-berlin.de
https://www.bcp.fu-berlin.de/en/chemie/biochemie/research-groups/knaus-group/index.html

University Education

  • 1980-1986  Studies of Biology, diploma, Universität Heidelberg
  • 1986-1991 Ph.D. thesis, Zentrum für Molekulare Biologie (ZMBH), Heidelberg
  • 1991 Ph.D. in Molecular Neurobiology

Professional Experience (selection)

  • 1991-1993 Postdoctoral research fellow, MIT, USA
  • 1993-1996 Postdoctoral associate, MIT, USA
  • 1996-2002 Research group leader (C1), Institute for Physiological Chemistry, Biocenter, Universität Würzburg
  • 2002 Venia legendi in Physiological Chemistry, Universität Würzburg
  • 2002-2004 Assistant Professorship (C2), Institute for Physiological Chemistry, Biocenter, Universität Würzburg
  • 2004 C3 Professor for Biochemistry, FU Berlin
  • Since 2010 W3 Professorship, Biochemistry and Molecular Basis of Regeneration, FU and Charité

Scientific Scope

Vascularization of tumors is a prerequisite for cancer progression and requires endothelial cell migration out of existing vessels, a process called angiogenesis. Most recent studies emphasize, that blood circulating BMPs (Bone or Body Morphogenetic Proteins) regulate in a dose dependent manner angiogenesis highlighting this pro-angiogenic function as novel clinical strategies for drug developments. The underlying molecular mechanism is however not understood. In our previous studies, we have unravelled the molecular mechanism, by which BMP2 and BMP14/GDF5 induce transcriptional and non-transcriptional responses in mesenchymal precursor cells. Using proteomics based approaches, we have identified a number of receptor associated proteins, which link to novel pathways, potentially involved in the regulation of cell migration, cytoskeletal rearrangements and cell-cell contact. We aim at providing novel strategies against tumor-induced angiogenesis and for innovative cancer therapies.

Selected References

  • Guzman, A, Zelman-Femiak, M, Boergermann, JH, Paschkowsky, S, Kreuzaler, PA, Fratzl, P, Harms GS, Knaus P. (2012) SMAD versus non-SMAD signalling is determined by lateral mobility of BMP receptors. J Biol Chem (in press)
  • Horbelt, D., Denkis, A., Knaus, P. (2011) A portrait of the TGF-ß/BMP family: Background matters. Int J Biochem Cell Biol. 2012 Mar; 44(3):469-74
  • Sieber, C., Kopf, J., Hiepen, C. and Knaus, P. (2009) Recent Advances in BMP Receptor Signaling. Cytokine and Growth Factor Rev 20(5-6): 343-55.
  • Schwappacher, R, Weiske, J, Heining, E, Ezerski, V, Marom, B, Henis, YI, Huber, O, and Knaus, P. (2009) Novel crosstalk to BMP signaling: cGMP-dependent kinase I modulates BMP receptor and Smad activity. EMBO J. 28(11):1537-50.
  • Bengtsson, L, Schwappacher, R. Roth, M., Hassel, S., and Knaus, P (2009) PP2A regulates BMP signalling by interacting with BMP receptor complexes and by dephosphorylating both the C-terminus and the linker region of Smad1. J. Cell Sci, 122(Pt 8):1248-57
  • Hartung, A., Bitton-Worms, K., Mouler Rechtman, M., Wenzel, V., Börgermann, J., Hassel, S., Henis, Y., Knaus, P. (2006) Different routes of BMP receptor endocytosis influence BMP signaling. Mol Cell Biol. 26(20): 7791-805.
  • Hassel, S., Eichner, A., Yakymovych, M., Hellman, U., Knaus, P., Souchelnytskyi, S. (2004) Proteins associated with type II bone morphogenetic protein receptor (BMPR-II) and identified by two-dimensional gel electrophoresis and mass spectrometry. Proteomics 4(5):1346-58.
  • Nohe, A., Haßel, S., Ehrlich, M., Neubauer, F., Sebald, W., Henis, Y. and Knaus, P. (2002). The mode of BMP receptor oligomerization determines different BMP-2 signaling pathways. J Biol Chem. 277(7):5330-8.
  • Rotzer, D., Roth, M., Lutz, M., Lindemann, D., Sebald, W. and Knaus, P. (2001). Type III TGF-ß Receptor independent signaling of TGF-ß2 via TßRII-B, an alternative spliced TGF-ß Type II Receptor. EMBO J. 20(3): 480-490
  • Gilboa, L., Nohe, A., Geissendörfer, T., Sebald, W., Henis Y. and Knaus, P. (2000). Bone morphogenetic protein receptor complexes on the surface of live cells: a new oligomerization mode for serine/threonine kinase receptors. Mol. Biol. Cell. 11(3): 1023-35.