Alternative interaction partners for arrestin. Although arrestin is principally involved in the inactivation of the visual pigment to quench phototransduction, it is clear that arrestin interacts with other proteins in photoreceptors to mediate other processes. Our lab was the first to demonstrate an intersection between phototransduction and glycolysis, demonstrating that arrestin binds enolase1 in rod and cone photoreceptors. This interaction modulates glycolysis by 25% which is a significant fraction for cells that consume 108 ATP/sec, half of which is produced by glycolysis. This finding has served as the central area in the development of a new therapy for treating retinal degenerative diseases. In addition, we showed that arrestin also binds to one of the Bardet-Biedl Syndrome proteins (BBS5). This finding is redefining how we look at the ancestral ciliary structure of the photoreceptor, identifying it as an important reservoir for a pool of proteins with ready access to the outer segment disc region of rods and cones.
- Bolch SN, Dugger DR, Chong T, McDowell JH, Smith WC (2016) A splice variant of Bardet-Biedl Syndrome 5 (BBS5) protein that is selectively expressed in retina. PLoS ONE 11: e0148773.
- Smith TS, Spitzbarth B, Li J, Dugger DR, Stern-Schneider G, Sehn E, Bolch SN, McDowell JH, Tipton J, Wolfrum U, Smith WC (2013) Light-dependent phosphorylation of Bardet Biedl Syndrome 5 in photoreceptor cells modulates its interaction with arrestin1. Cell Mol Life Sci 70:4603-4616. PMC3819411
- Smith WC, Bolch SN, Dugger DR, Li J, Esquenazi I, Arendt A, Benzenhafer D, McDowell JH (2011) Interaction of arrestin with enolase1 in photoreceptors. Invest. Ophthalmol. Vis. Sci. 52(3):1832-40.