Professor Emeritus of Cell and Developmental Biology*
*And Affiliate, Division of Neurobiology
Our lab has investigated the roles of the actin cytoskeleton in morphogenesis and survival of vertebrate retinal photoreceptors. These studies contribute to our understanding of human vision and the prevention of blindness. Though research still continues in collaborations, Dr. Burnside has closed the lab at Berkeley and is no longer taking students or post-docs.
Most recently we have studied two proteins associated with the elaborately polarized actin cytoskeletons of photoreceptors: the motor protein myosin 3A and the actin filament cross-linker fascin 2.
Class III myosins are unusual unconventional myosins. Although they have motor domains and bind actin like other myosins, they differ from all other myosins in having a kinase domain N-terminal to the motor domain. The presence of the kinase suggests that class III myosins play roles in cell signaling as well as in cell motility. Drosophila NINAC, the first class III myosin to be discovered, was initially identified as the defective gene responsible for causing photoreceptor degeneration in flies. Our lab cloned the first vertebrate homologues of NINAC to be identified, and showed that two homologues of this motor, Myo3A and Myo3B, are highly expressed in vertebrate photoreceptors, where they are localized to microvillus-like processes that cup the base of the photopigment-bearing outer segment. Myo3A is also expressed in the hair cells of the inner ear, the cells responsible for hearing. Mutations in Myo3A lead to deafness but not blindness, perhaps because Myo3B is also present in photoreceptors and can compensate for the loss of Myo3A function.
Fascin 2 is a retinal-specific member of the fascin family of actin-binding proteins. Fascins are cross-linkers that bundle actin filaments. Fascin 2 mutation in humans results in autosomal dominant retinitis pigmentosa and macular dystrophy (Wada et al. (2001) IOVS 42:2395-2400, Wada et al. (2003) Ophth. Mol. Gen. 121:1613-1620), suggesting an important role for fascin 2 in photoreceptor survival. We have analyzed the subcellular location of fascin 2 in photoreceptors using immunohistochemistry and GFP-tagged fascin 2 transgenes in Xenopus tadpole rods, have analyzed retinal fascin actin-binding properties in vitro. These studies were directed toward ascertaining the role fascin plays in photoreceptor development and function.
Mouse class III myosins: kinase activity and phosphorylation sites. J.S.Dalal, S.M. Steven, Jr., S. Alverez, N. Munoz, N., K.E.Kempler, A.C. Dose, B. Burnside, and B-A Battelle. (2011) Neurochem. 10.1111/j.1471-4159.2011.07468.x (pp.1-13).
Fascin 2b is a component of stereocilia that lengthens actin-based protrusions. S. Chou, P.S. Hwang, G, Gomez, C.A. Fernando, M.C. West, L.M. Pollack, J.Lin-Jones, B. Burnside, and B.M. McDermott, Jr (2011) PLoS ONE 6:e14807 (pp1-13).
Fish retinomotor movements. B. Burnside and C. Kingsmith. (2010) In D. A. Dartt, J. Besharse, and R. Danz, (Eds.) Encyclopedia of the Eye, vol. 2. Oxford:Academic Press. pp. 142-150.
Cloning and distribution of myosin 3B in the mouse retina: differential distribution in cone outer segments. C. Katti, J.S. Dalal, A.C. Dose, B. Burnside, and B. Batelle. (2009) Exp. Eye Res. 89:224-237
Identification and localization of myosin superfamily members in fish retina and retinal pigment epithelium. J. Lin-Jones, L. Sohlberg, A. Dose, J. Breckler, D.W. Hillman, and B. Burnside. (2009) J. Comp. Neurol. 513:209-233.
Retinomotor movements. B. Burnside and C. King-Smith.(2009) In Encyclopedia of Neuroscience, Larry R. Squire. (ed.). Oxford:Academic Press. http://www.sciencedirect.com/science/referenceworks/9780080450469 (accessed July 2009) pp. 275-281.Class III Myosins. A.C. Dosé, J. Lin-Jones, and B. Burnside. (2008) In: “Myosins, A Superfamily of Molecular Motors,” L. Coluccio. (ed.) Springer Publishing Company, pp.265-288.
The kinase domain alters the kinetics of the myosin IIIA motor. A.C. Dosé, S. Ananthanarayanan, J.E.Moore, A.C. Corsa, B. Burnside, and C.M.Yengo (2008) Biochemistry 47(8):2485-96.
The retina-specific protein, fascin 2 is an actin crosslinker associated with actin bundles in photoreceptor inner segments and calycal processes. J. Lin-Jones and B. Burnside (2007). IOVS. 48(3): 1380-8.
The kinetic mechanism of human myosin IIIA. A.C. Dose, S. Ananthanarayanan, J.E. Moore, B. Burnside, C.M. Yengo (2006) J. Biol. Chem. 104 (3) 772-7.
A new compartment at stereocilia tips defined by spatial and temporal patterns of myosin IIIa expression. M.E. Schneider, A.C. Dose, F.T. Salles, W. Chang, F.L. Erickson, B. Burnside, B. Kachar (2006) J. Neuroscience. 26(40):10243-52.
Characterization of peripherin/rds and rom-1 transport in rod photoreceptors of transgenic and knockout animals. E.S. Lee, B. Burnside, J.G. Flannery. (2006) Inv. Ophthal. Vision Sci. 47(5):2150-2160.
Myosin VI is required for structural integrity of the apical surface of sensory hair cells in zebrafish. C. Seiler, O. Ben-David, S. Sidi, O. Hendrich, A. Rusch, B. Burnside, K.B. Avraham, T. Nicolson (2004). Dev. Biol. 272(2):328-338.
Myosin III in photoreceptors: What does it do? A.C. Dose, J. Lin-Jones, and B. Burnside (2004) In: Photoreceptor Cell Bilogy and Inherited Retinal Degenerations (ed.) D.S. Williams, World Scientific Publishing, Singapore, 2004, pp. 351-370.
Myosin 3A transgene expression produces abnormal actin filament bundles in transgenic Xenopus laevis rod photoreceptors. J. Lin-Jones, E. Parker, M. Wu, A. Dose, and B. Burnside (2004) J. Cell. Sci. 117:5825-5834.
Last Updated 2009-11-30