Research Activities
Our goal is to understand the molecular mechanism of synaptic neurotransmission. We are interested in the structure, function, and dynamics of key players in the synaptic vesicle fusion machinery. Our lab is also working on the mechanism of action of clostridial neurotoxins that target this machinery. Other projects include protein complexes that are involved in synaptic development and the ATPases of the AAA family that are involved in protein complex disassembly and degradation. A molecular understanding of these complex protein machineries may ultimately lead to new therapeutics to treat human diseases.
Selected Projects Recent Publications

schematic diagram of how synaptic vesicle fusion occurs assisted by SNAREs

Synaptic Vesicle Fusion

Diagram of BoNTA light chain on the surface of a cell

Mechanism of Clostridial Neurotoxins

  J.M.Davies, A.T.Brunger, W.I.Weis, Improved structures of full-length p97, an AAA ATPase: implications for mechanisms of nucleotide-dependent conformational change. Structure 16, 715-726, 2008.

 A.T.Brunger, R.Jin, M.A.Breidenbach, Highly specific interactions between botulinum neurotoxins and synaptic vesicle proteins. Cell.Mol.Life Sci., online (2008)

 K.Weninger, M.E.Bowen, U.B.Choi, S.Chu, and A.T.Brunger, Accessory proteins stabilize the acceptor complex for synaptobrevin, the 1:1 syntaxin/SNAP-25 complex. Structure 16, 308-320 (2008).

 A.Schweizer Burguete, T.D.Fenn, A.T.Brunger, and S.R.Pfeffer, Rab and Arl GTPase family members cooperate in the localization of the Golgin GCC185. Cell 132, 286-298 (2008).

 P.Strop, S.E.Kaiser, M.Vrljic, and A.T.Brunger. The structure of the yeast plasma membrane SNARE complex reveals destabilizing water filled cavities. J. Biol. Chem, 283, 1113-1119 (2008).

 D.Arac, A.A.Boucard, E.Ozkan, P.Strop, E.Newell, T.C.Sudhof, A.T.Brunger. Structures of Neuroligin-1 and the Neuroligin-1/Neurexin-1b complex reveal specific protein-protein and protein-Ca2+ interactions. Neuron 56, 992-1003 (2007).

 D.M.Pinkas, P.Strop, A.T.Brunger, C.Koshla, Transglutaminase 2 undergoes a large conformational change upon activation. PLOS Biology 5 2788-2796 (2007).

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