Fasshauer, Dirk, Dr.#

Independent Research Group Leader - Structural Biochemistry

  • 1994 Doctoral degree (Dr. rer. nat.) University of Göttingen
  • 1995-97 Postdoctoral fellow, Yale University
  • since 1997 Postdoctoral fellow, Dept. for Neurobiology, Max Planck Institute for Biophysical Chemistry, Göttingen
  • since 2002 Group leader within the Dept. for Neurobiology, Max Planck Institute for Biophysical Chemistry, Göttingen
  • since 2006 Independent Research Group Leader, Structural Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen

Major Research Interests

The mechanism by which eukaryotic cells transport material between intracellular organelles is of fundamental importance in cell biology. Transport is mediated by vesicles that bud from a donor organelle and afterwards fuse with a target organelle. Currently, it is becoming clear that the underlying molecular machineries involved in the principal aspects of vesicular trafficking are highly conserved among all eukaryotes. Key players during the final step in vesicle trafficking, the fusion of a vesicle with its acceptor membrane, are the so-called SNARE proteins. SNARE proteins are thought to assemble into a tight complex between the fusing membranes, pulling them together (the ‘zipper’ model). To come to a better understanding of the molecular events during vesicular fusion, we focus on a detailed structural, kinetic, thermodynamic, and phylogenetic characterization of the underlying protein-protein interactions. In particular, we want to investigate how SNARE assembly takes place, how this process is controlled and catalyzed by other factors. Next to standard biochemical techniques, we employ spectroscopic (Circular Dichroism and Fluorescence Spectroscopy) and calorimetric (Isothermal Titration Calorimetry) methods.

Homepage Department/Research Group:

Selected Recent Publications

  • Winter U, Chen X, Fasshauer D (2009) A conserved membrane attachment site in alpha-SNAP facilitates N-ethylmaleimide-sensitive factor (NSF)-driven SNARE complex disassembly. J Biol Chem 284(46):31817-26
  • Wiederhold K, Fasshauer D (2009) Is assembly of the SNARE complex enough to fuel membrane fusion? J Biol Chem 284(19):13143-52
  • Fasshauer D, Jahn R (2007) Budding insights on cell polarity. Nat Struct Mol Biol 14(5):360-2
  • Kloepper, T.H., Kienle, C.N., and Fasshauer, D. (2007). An elaborate classification of SNARE proteins sheds light on the conservation of the eukaryotic endomembrane system. Mol. Biol. Cell 18: 3463-71
  • Pobbati A, Stein A, Fasshauer D (2006) N- to C-terminal SNARE complex assembly promotes rapid membrane fusion. Science 313:673-6
  • Soerensen JB, Wiederhold K, Müller EM, Milosevic I, Nagy G, de Groot BL, Grubmüller H, Fasshauer D (2006) Sequential N- to C-terminal ‘zipping-up’ of the SNARE complex drives priming and fusion of secretory vesicles. EMBO J 25:955-66
  • Pobbati A, Razeto A, Böddener M, Becker S, Fasshauer D (2004) A structural basis for the inhibitory role of tomosyn in exocytosis. J Biol Chem 279:47192-200
  • Fasshauer D, Antonin W, Subramaniam V, Jahn R (2002) SNARE assembly and disassembly exhibit a pronounced hysteresis. Nat Struct Biol 9:144-151