Reisinger, Ellen, PD Dr.*

Junior Group Leader, Otorhinolaryngology & InnerEarLab

  • 2000: Diploma in Biochemistry, University of Tübingen
  • 2001-2005:Experimental PhD thesis work in the Department of Physiology II University of Freiburg, Germany
  • 2005: PhD degree of the Faculty of Biology, University of Freiburg
  • 2005-2006: Postdoctoral Research Fellow, Department of Physiology II, University of Freiburg
  • 2006-2007: Postdoctoral Research Fellow, Department of Otolaryngology, University of Göttingen, and Department for Molecular Neurobiology of the Max-Planck-Institute for Experimental Medicine, Göttingen
  • 2007- today:Head of the Molecular Biology of Cochlear Neurotransmission junior research group, University of Göttingen

Major Research Interests

With my group I aim to unravel molecular mechanisms playing a role for hearing and deafness. Specifically, we focus on the mechanism and pathomechanism of synaptic transmission in auditory hair cells. The protein otoferlin is known to be essential for a late step of vesicle exocytosis (Roux et al., Cell 2006). To date, it is largely unknown how otoferlin triggers exocytosis or regulates vesicle replenishment. Our group studies the impact of pathogenic missense mutations in otoferlin on the protein function in mouse models (as in Pangrsic et al., Nat Neurosci 2010). Further, we aim to understand the role of the individual protein domains in otoferlin by solving the structure of these and by testing the biochemical properties, like binding to Ca2+, phospholipid membranes or other proteins. Recently, we solved the structure of the most N-terminal C2 domain of otoferlin by X-ray crystallography, for which we collaborate with Ralf Ficner’s group at the Dept. for Molecular Structural Biology. Using viral transduction of hair cells, we could express synaptotagmin-1, the major Ca2+ sensor for exocytosis in central nervous system synapses, in auditory hair cells of otoferlin knock-out mice. That way, we could demonstrate that otoferlin and synaptotagmin-1 cannot functionally replace each other, challenging the hypothesis of otoferlin being a Ca2+ sensor for vesicle fusion. Currently, we aim to transduce otoferlin knock-out hair cells with full length otoferlin cDNA, such that we can study the effect of mutations in otoferlin on synaptic function. Our goal is to analyze the function of the individual protein domains and the role of their Ca2+ binding sites by patch clamp of the transduced hair cells and by immunhistochemical analysis of protein levels and cellular distribution.

Homepage Department/Research Group

Selected Recent Publications

  • Hammerschmidt K, Reisinger E, Westekämper K, Ehrenreich L, Strenzke N, Fischer J (2012) Mice do not require auditory input for the normal development of their ultrasonic vocalizations. (in press in BMC Neuroscience)
  • Reisinger E, Bresee C, Neef J, Nair R, Reuter K, Bulankina AV, Nouvian R, Koch M, Bückers J, Kastrup L, Roux I, Petit C, Hell SW, Brose N, Rhee JS, Kügler S, Brigande JV, Moser T (2011) Probing the functional equivalence of otoferlin and synaptotagmin 1 in exocytosis. J Neurosci 31(13): 4886-4895
  • Helfmann S, Neumann P, Tittmann K, Moser T, Ficner R, Reisinger E (2011) The Crystal Structure of the C2A Domain of Otoferlin Reveals an Unconventional Top Loop Region. J Mol Biol 406: 479-490
  • Reisinger E, Meintrup D, Oliver D, Fakler B (2010) Gene expression associated with the onset of hearing detected by differential display in rat organ of Corti. Eur J Hum Genetics 18(12):1327-32
  • Pangršič T, Lasarow L, Reuter K, Takago H, Schwander M, Riedel D, Frank T, Tarantino LM, Bailey JS, Strenzke N, Müller U, Brose N, Reisinger E*, Moser T* (2010) Hearing requires otoferlin-dependent efficient replenishment of synaptic vesicles in hair cells. Nature Neurosci 13(7): 869-76 (* shared correspondence)