Research

The brain is extremely complex. An estimated hundred billion neurons in the human brain make hundreds of trillions of connections (synapses). Synapses come and go. Synapses grow "weaker" and "stronger", as their adhesive properties and their ability to transmit signals changes (Goda & Davis (2003) Neuron 40:242-64).

Synapses change in response to activity. Outside stimuli triggering memory and learning or stress, as well as exposure to certain chemicals such as drugs of abuse, anti-depressants and anti-psychotics, can change the shape and number of neurons and their connections (Duman (2002) European Psychiatry 17 Supplement 3:306-10).

There is a huge network of proteins that are recruited to the synapse. Their molecular interactions are just starting to be revealed. Click on the image for a larger view of the proteins involved in the synapse.

[image source: Rao, A., Harms, K. J., & Craig, A. M. (2000). Neuroligation: building synapses around the neurexin-neuroligin link. Nature Neuroscience, 3, 747-49.]

The Rudenko lab uses structural biology and biophysical techniques to understand protein molecules involved in

• formation and maintenance of synapses
• neuron:neuron recognition
• neuron:neuron adhesion
• recruitment of receptors and channels to the synapse
• response to
• stress
• drugs of abuse
• certain treatments used for mental illness

Understanding how proteins look in three dimensions (their chemical formula) helps us understand how these proteins work in the cell to carry out their function. We determine the structure of proteins by x-ray crystallography.

To learn more about what we do, or if there is an interesting protein you would like to crystallize, feel free to visit the Rudenko lab on the third floor of the Life Sciences Institute.