The long term goal of this application is to determine how a membrane protein, in this case prestin, found in cochlear outer hair cells (OHCs), can enable voltage-induced cell deformation. To this end, we will study protein-protein, protein-lipid, and membrane-cytoskeleton interactions. To understand how prestin affects membrane deformation, we will study the behavior of membrane molecules under perturbation using an optical technique called fluorescence polarization microscopy (FPM). We will also study how molecules that comprise the cytoskeleton behave under deformation using the same technique. Lastly, though prestin is widely accepted as the membrane motor protein in OHCs, little is known about its mechanism of action. We hypothesize that prestin may be interacting with itself or other membrane proteins to induce length changes and propose to use fluorescence resonance energy transfer to quantify the degree of interaction. The results from each of these proposed studies will further elucidate prestin's role in electromotility and its function as a membrane protein.
| Greeson, Jennifer N; Raphael, Robert M (2009) Amphipath-induced nanoscale changes in outer hair cell plasma membrane curvature. Biophys J 96:510-20 |
| Rajagopalan, Lavanya; Greeson, Jennifer N; Xia, Anping et al. (2007) Tuning of the outer hair cell motor by membrane cholesterol. J Biol Chem 282:36659-70 |
| Greeson, Jennifer N; Raphael, Robert M (2007) Application of fluorescence polarization microscopy to measure fluorophore orientation in the outer hair cell plasma membrane. J Biomed Opt 12:021002 |
| Greeson, Jennifer N; Organ, Louise E; Pereira, Fred A et al. (2006) Assessment of prestin self-association using fluorescence resonance energy transfer. Brain Res 1091:140-50 |
