Jahn, Reinhard, Prof. Dr.
Professor, Director at the Max Planck Institute for Biophysical Chemistry
- Dr. rer. nat., University of Göttingen, Germany, 1981
- Assistant Professor, The Rockefeller University, New York, USA, 1985
- Junior Group Leader, Max Planck Institute for Psychiatry, Martinsried, Germany, 1986
- Associate Professor of Pharmacology and Cell Biology, Yale University, and Investigator, Howard Hughes Medical Institute, New Haven, USA, 1991
- Professor of Pharmacology and Cell Biology, Yale University, New Haven, 1995
- Director of the Department of Neurobiology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany, 1997
Major Research Interests
Our group is interested in the mechanisms of membrane fusion, with the main emphasis on regulated exocytosis in neurons. Since recent years it is known that intracellular membrane fusion events are mediated by a set of conserved membrane proteins, termed SNAREs. For fusion to occur, complementary sets of SNAREs need to be present on both of the fusing membranes. The neuronal SNAREs are among the best characterized. They are the targets of the toxins responsible for botulism and tetanus. To understand how these proteins make membranes fuse, we studied their properties in detail using biochemical and biophysical approaches. We found that they assemble into a tight complex which ties the membrane closely together and thus probably initiates bilayer mixing.
In our current approaches, we study membrane fusion at the level of isolated proteins as well as in semi-intact and intact cells. Thus, we are investigating conformational changes of the SNARE proteins before and during fusion. Furthermore, we use reconstitution of membrane fusion in cell-free assays and in proteoliposomes. Other projects of the group include the study of neurotransmitter uptake by synaptic vesicles and the function of Rab-GTPases in neuronal exocytosis.
Homepage Department/Research Group
http://www.mpibpc.mpg.de/groups/jahn/
Selected Recent Publications
- van den Bogaart G, Meyenberg K, Risselada JH, Amin H, Willig KI, Hubrich BE, Dier M, Hell SW, Grubmüller H, Diederichsen U, Jahn R. Membrane protein sequestering by ionic protein-lipid interactions. Nature, in press
- van den Bogaart G, Thutupalli S, Risselada JH, Meyenberg K, Holt M, Riedel D, Diederichsen U, Herminghaus S, Grubmüller H, Jahn R (2011) Synaptotagmin-1 may be a distance regulator acting upstream of SNARE nucleation. Nat. Struct. Mol. Biol. 18, 805-812
- Pavlos NJ, Grønborg M, Riedel D, Chua JJE, Boyken J, Kloepper TH, Urlaub H, Rizzoli SO, Jahn R (2010) Quantitative analysis of synaptic vesicle Rabs uncovers distinct yet overlapping roles for Rab3a and Rab27b in Ca2+-triggered exocytosis. J Neurosci 30(40):13441-13453
- Chua JJ, Kindler S, Boyken J, Jahn R (2010) The architecture of an excitatory synapse. J Cell Sci 123: 819-823
- Barysch SV, Aggarwal S, Jahn R, Rizzoli SO (2009) Sorting in early endosomes: connections to docking and fusion-associated factors. Proc Natl Acad Sci USA 106: 9697-9702
- Van den Bogaart G, Holt MG, Bunt G, Riedel D, Wouters FS, Jahn R (2009) One SNARE complex is sufficient for membrane fusion. Nat Struct Mol Biol 17: 358-364
- Grønborg M, Pavlos NJ, Brunk I, Chua JJE, Münster-Wandowski A, Riedel D, Ahnert-Hilger G, Urlaub H, Jahn R (2009) Quantitative comparison of glutamatergic and GABAergic synaptic vesicles unveils selectivity for few proteins including MAL2, a novel synaptic vesicle protein. J Neurosci 30: 2-12
- Stein A, Weber G, Wahl MC, Jahn R (2009) Helical extension of the neuronal SNARE complex into the membrane. Nature 460: 525-528
- Holt M, Riedel D, Stein A, Schuette C, Jahn R (2008) Synaptic vesicles are constitutively active fusion machines, which function independently of Ca2+. Curr Biol 18: 715-722
- Takamori S, Holt M, Stenius K, Lemke EA, Grønborg M, Riedel D, Urlaub H, Schenck S, Brügger B, Ringler P, Müller SA, Rammner B, Gräter F, Hub JS, De Groot BL, Mieskes G, Moriyama Y, Klingauf J, Grubmüller H, Heuser J, Wieland F, Jahn R (2006) Molecular anatomy of a trafficking organelle. Cell 127: 831-846