CopA is an ATP-dependent Cu+ pump belonging to the family of P-type ion pumps. YiiP is a Zn2+ transporter belonging to the Cation Diffusion Facilitator (CDF) family. The Stokes lab used methods of helical reconstruction to solve 3D structures of both proteins.

The Suh lab is working to understand how neural circuits generate innate behavior in Drosophila using molecular genetic tools, calcium imaging techniques with a live, behaving fly preparation, and quantitative behavioral assays.

The Traaseth lab is focused on revealing the transport mechanism of membrane proteins through determination of their structures. Theirbroader interest is in engineering new drugs and proteins that elicit tailored biological responses.

Dr Tsien's lab is studying how the location and identity of presynaptic calcium channels is regulated. Voltage-gated Ca2+ channels provide the critical link between the firing of a presynaptic nerve terminal and its release of neurotransmitter. The Ca2+ channels must be positioned very close to sites of vesicle fusion, and come in diverse forms with distinct activity-dependence, responsiveness to GABA, dopamine, acetylcholine and other neuromodulators, and susceptibility to neurological disorders such as migraine, ataxia or dystonia. Our working hypothesis involves molecular "slots" for particular types of channels. Slots regulate the mix of channel types and also help explain how defective channels might displace normal ones in genetically dominant disorders.

The Wang laboratory aims to understand the molecular mechanisms of membrane transporters and channels by structural, biochemical & biophysical approaches. Recently, they determined the structures of the formate channel FocA from Vibrio cholerae, without and with formate ions bound.

AMPA receptors and pain; AMPA receptor trafficking

The Ziff lab studies the molecular mechanisms which regulate synaptic transmission at excitatory synapses. They focus on two ion channels, the AMPA and the NMDA type glutamate receptors.They have cloned proteins which associate with the cytoplasmic tail of the GluR2 AMPA type glutamate receptor subunit and are studying the role of these binding factors in receptor control.