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

http://www.uni-bc.gwdg.de/index.php?id=306

Selected publications

James C, Möller U, Spillner C, König S, Dybkov O, Urlaub H, Lenz C, Kehlenbach RH (2024). Phosphorylation of ELYS promotes its interaction with VAPB at decondensing chromosomes during mitosis. EMBO Rep.

Kehlenbach RH, Neumann P, Ficner R, Dickmanns A (2023). Interactions of nucleoporins with nuclear transport receptors: a structural perspective. Biol. Chem. Biol. Chem. 404, 791-805

Pörschke M, Rodríguez-González I, Parfentev I, Urlaub, H, Kehlenbach RH (2023). Transportin 1 is a major nuclear import receptor of the nitric oxide synthase interacting protein. J Biol Chem.
J Biol Chem. 299, 102932

Lagadec F, Carlon-Andres I, Ragues J, Port S, Wodrich H, Kehlenbach RH (2022). CRM1 Promotes Capsid Disassembly and Nuclear Envelope Translocation of Adenovirus Independently of Its Export Function. J Virol. 96(3): e0127321

Baade I, Hutten S, Sternburg EL, Pörschke, M, Hofweber M, Dormann D* and Kehlenbach RH* (2021). The RNA-binding protein FUS is chaperoned and imported into the nucleus by a network of import receptors. J Biol. Chem. 296, 100659*, co-corresponding

Hamed M, Caspar B, Port SA and Kehlenbach RH (2021). A nuclear export sequence in Nup214 promotes CRM1-dependent targeting of the nucleoporin to the nuclear pore complex. J Cell Sci. 134. doi: 10.1242/jcs.258095

Ashkenazy-Titelman A, Shav-Tal Y* and Kehlenbach RH* (2020). Into the basket and beyond – the journey of mRNA through the nuclear pore complex. Biochem. J. 477, 23-44. *, co-corresponding

James C, Müller M, Goldberg, MW, Lenz C, Urlaub H and Kehlenbach RH (2019). Proteomic mapping by rapamycin-dependent targeting of APEX2 identifies binding partners of VAPB at the inner nuclear membrane. J. Biol. Chem. 294, 16241-16254

Baade I and Kehlenbach RH. (2019). The cargo spectrum of nuclear transport receptors. Curr Opin Cell Biol. 58, 1-7

Baade I, Spillner C, Schmitt, K, Valerius, O and Kehlenbach RH (2018). Extensive identification and in-depth validation of importin 13 cargoes. Mol. Cell. Proteomics 17, 1337-1353.

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. *, co-corresponding

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. *, co-corresponding