
Michael Richters and Rachelle Gaudet dance a routine they choreographed to illustrate our research on TRPV1 ion channels. TRPV1 channels are proteins in the cell membrane of neurons that innervate the skin. Upon sensing hot temperature, they open a pore that lets ions cross the membrane and thereby generate an electrical signal. This signal is eventually transmitted to the brain, generating a painfully hot message. Anecdotally, TRPV1 channels are also activated (opened) by the capsaicin chemical found in chili peppers, explaining their hot taste. The lab's long term goal is to determine the three-dimensional structure of TRPV1 to understand how it functions. In the process, we have discovered mechanisms involved in TRPV1 desensitization, when it is inactivated over time, through closure of the pore, even in the presence of an activating signal.
In the routine, Rachelle and Mike use three American dances from the 1920s and 1930s that are performed to big band swing music: first, Balboa, which developed in southern California; second, Lindy Hop, the original form of Swing that grew out of the Savoy Ballroom in Harlem; and finally, Collegiate Shag, which is thought to have originated in Louisiana.
You will witness the protein fold into its closed state and then diffuse along the neuron membrane (or dance floor), illustrated by the Balboa dance. As the temperature rises (notice how the tempo, representing the temperature or kinetic energy in the system, increases throughout the song), the TRPV1 channel is activated and opens, represented by the switch to Lindy Hop. The TRPV1 protein eventually desensitizes, closing again, as illustrated by the Collegiate Shag. Finally, as the temperature increases too much, the protein denatures and unfolds...
Michael Richters (aka transducin beta-gamma) and Rachelle Gaudet (aka phosducin) use Lindy Hop and Charleston to illustrate Rachelle's PhD thesis: Structural analysis of phosducin and its phosphorylation-regulated interaction with transducin beta-gamma. These proteins function in our eyes, as part of the retinal proteins that transmit visual signals to the brain. In a bright environment, phosducin binds to transducin beta-gamma and the two are found in the cytoplasm. Upon dark-adaptation, phosducin becomes phosphorylated, while transducin beta-gamma returns to the cellular membranes to increase the responses to small amounts of light.
During Rachelle's PhD, she determined the crystal structure of the complex of phosducin and transducin beta-gamma. In this complex, phosducin's N-terminal half interacts extensively with beta-gamma, illustrated in the Lindy Hop, a partner dance which relies on intricate lead-follow technique. They dance the Lindy Hop under bright lights in the back of the room, because the complex phosducin/transducin beta-gamma forms when our eyes are adapted to bright light. When eyes adapt to the dark (illustrated by our transition to the darkened front of the room), phosducin is released from beta-gamma and becomes phosphorylated (represented by the hat). In the second half of her thesis project, Rachelle went on to show that phosphorylated phosducin has a particularly flexible or mobile N-terminal half. This is illustrated by the solo Charleston dance, which features big arm movements. Upon return to the light, phosducin loses its phosphorylation and returns to its interaction with beta-gamma. The dark-light cycles continue until beta-gamma is targeted for destruction. Finally, the song choice speaks for itself!
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Last Updated: 5-29-09