Structure of proteins involved in synaptic vesicle fusion in neurons.
The fusion of vesicles with target membranes is controlled by a complex network of protein-protein and protein-lipid interactions. Structures of the SNARE complex, synaptotagmin III, nSec1, domains of the NSF chaperone and its adaptor SNAP, and Rab3 and some of its effectors provide the framework for developing molecular models of vesicle fusion and for designing experiments to test these models.
Brunger
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The Howard Hughes Medical Institute and Department of Molecular and Cellular Physiology, Neurology and Neurological Sciences, and Stanford Synchrotron Radiation Laboratory, Stanford University, Stanford, California 94305, USA. axel.brunger@stanford.edu
D000818:Animals; D002135:Calcium-Binding Proteins; D002352:Carrier Proteins / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism*; D006801:Humans; D008562:Membrane Glycoproteins / Q000378:metabolism; D008958:Models, Molecular; D052066:N-Ethylmaleimide-Sensitive Proteins; D009419:Nerve Tissue Proteins / Q000378:metabolism; D009474:Neurons / Q000737:chemistry* / Q000502:physiology*; D011485:Protein Binding; D013569:Synapses / Q000502:physiology*; D050857:Synaptotagmins; D033921:Vesicular Transport Proteins; D020692:rab3 GTP-Binding Proteins / Q000378:metabolism
D002135:Calcium-Binding Proteins; D002352:Carrier Proteins; D008562:Membrane Glycoproteins; D009419:Nerve Tissue Proteins; C494288:SYT3 protein, human; D033921:Vesicular Transport Proteins; D050857:Synaptotagmins; D052066:N-Ethylmaleimide-Sensitive Proteins; D020692:rab3 GTP-Binding Proteins