Axel Brunger is interested in the molecular mechanisms behind the release of neurotransmitters when synaptic vesicles fuse with active zones of presynaptic neurons and how these mechanisms relate to physiological function. To capture and study the protein machinery at work, Brunger and his team determine 3-D structures or images from atomic to cellular resolutions. These structures then frame further investigations involving biophysical methods, optical microscopy, and experimentation in live neurons to explore the functional and dynamic aspects of neurotransmitter release. The team’s work may provide possible targets for therapeutics.
New HHMI research reveals how three proteins help brain cells synchronize the release of chemical signals. A similar interaction may play a role in how cells secrete insulin and airway mucus, too. Scientists have determined new structures of an essential cellular recycling machine with near atomic-level detail. The structures, which show a protein called NSF alone and interacting with its target, a protein complex called SNARE that is formed when membranes fuse together.