Kehlenbach, Ralph, Prof. Dr.
Professor, Department of Molecular Biology
- Diploma in biology, University of Bonn, 1992
- Dr. rer. nat., University of Heidelberg, 1995
- Postdoctoral fellow, The Scripps Research Institute, USA, 1996-2000
- Group leader University of Heidelberg, 2000-2004
- Group leader University of Göttingen, since 2005
- Habilitation in Biochemistry and Molecular Biology, 2007
Major Research Interests
Transport of macromolecules between the nucleus and the cytoplasm occurs through nuclear pore complexes (NPCs), large supramolecular structures that are embedded between the outer and the inner nuclear membrane. Whereas small molecules (< 40 kDa) may passively diffuse through the NPC, nuclear transport of larger proteins or nucleic acids is an energy-dependent, signal-mediated process.
We are characterizing the function of several nuclear transport receptors with a particular focus on CRM1, the major export receptor for transport of proteins as well as different RNA species out of the nucleus. Furthermore, we are analyzing the transport mechanisms of proteins that are targeted to the inner nuclear membrane. Finally, we are interested in the role of individual nucleoporins in nuclear transport of soluble and membrane-bound proteins. For our analyses, we use a large variety of structural, biochemical and cell biological approaches.
Homepage Department/Research Group
- Pfaff J, Rivera Monroy, J, Jamieson, C, Rajanala, K, Vilardi, F, Schwappach B, and Kehlenbach RH (2016). Emery-Dreifuss muscular dystrophy mutations impair TRC40-mediated targeting of emerin to the inner nuclear membrane. J Cell Sci. 129, 502-516
- Port, SA, Monecke, T, Dickmanns, A, Spillner, C, Hofele, R, Urlaub, H, Ficner, R, and Kehlenbach, RH (2015). Structural and functional characterization of CRM1-Nup214 interactions reveals multiple FG-binding sites involved in nuclear export. Cell Rep. 13, 690-702
- Dickmanns, A, Kehlenbach, RH, and Fahrenkrog, B. (2015). Nuclear pore complexes and nucleocytoplasmic transport: from structure to function to disease. Int. Rev. Cell Mol. Biol. 320, 171-233
- Kimura M, Thakar K, Karaca S, Imamoto N, and Kehlenbach RH. (2014). Novel approaches for the identification of nuclear transport receptor substrates. Methods Cell Biol. 122, 353-378.
- Roloff, S., Spillner, C., and Kehlenbach, R.H. (2013). Several phenylalanine-glycine motives in the nucleoporin Nup214 are essential for binding of the nuclear export receptor CRM1. J. Biol. Chem. 288, 3952-3963.
- Thakar, K., Karaca, S., Port, S. A., Urlaub, H. and Kehlenbach, R. H. (2013). Identification of CRM1-dependent nuclear export cargoes using quantitative mass spectrometry. Mol. Cell. Proteomics. 12, 664-678.
- Wälde, S., Thakar, K., Hutten, S., Spillner, C., Nath, A. Rothbauer, U., Wiemann, S., and Kehlenbach, R.H. (2012). The nucleoporin Nup358/RanBP2 promotes nuclear import in a cargo- and transport receptor-specific manner. Traffic. 13, 218-233.
- Waldmann, I, Spillner, C., and Kehlenbach, R.H. (2012). The nucleoporin like protein NLP1/hCG1 promotes CRM1-dependent nuclear protein export. J. Cell Science. 124, 144-154.