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Beth Burnside

Beth Burnside

Professor Emerita of Cell and Developmental Biology*
*And Affiliate, Division of Neurobiology

Lab Homepage: http://mcb.berkeley.edu/labs/burnside/

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Research Interests

Our lab is investigating the roles of the actin cytoskeleton in the morphogenesis and survival of vertebrate retinal photoreceptors. These studies contribute to our understanding of  human vision and the prevention of blindness.

Current Projects

Currently, we are studying 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. We are now investigating the functions of Myo3A and Myo3B in photoreceptors by a variety of approaches, including heterologous expression in cultured cells, transgenic expression in Xenopus photoreceptors, and biochemical and molecular characterization of human and fish Myo3A kinase, motor, and tail domains.

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. Currently we are analyzing the subcellular location of fascin 2 in photoreceptors using immunohistochemistry and GFP-tagged fascin 2 transgenes in Xenopus tadpole rods, analyzing retinal fascin actin-binding properties in vitro, and trying to ascertain the role fascin plays in photoreceptor development and function.

Selected Publications

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.

Forging successful university-industry collaborations: replacing adversarial dialogue with engagement can bridge the cultural gap. B. Burnside and L.Witkin (2008) Research-Technology Management 52(2):26-30. 

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.

Retinomotor movements. B. Burnside and C. King-Smith (2008) In: Squire, L. (Editor in Chief) New Encyclopedia of Neuroscience. Academic Press, Oxford.

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) IOVS 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.

Disruption of Kinesin II Function Using a Dominant Negative-Acting Transgene in Xenopus laevis Rods Results in Photoreceptors Degenerations. J. Lin-Jones, E. Parker, M. Wu, B.E. Knox, and B. Burnside (2003) IOVS 44:3614-3621.

Localization of a Class III Myosin to Filopodia Tips in Transfected HeLa Cells Require an Actin-binding Site in its Tail Domain. F.L. Erickson, A.C. Corsa, A.C. Dose, and B. Burnside (2003) Mol. Biol. Cell. 14:1058-1073.

Myo3A, One of Two Class III Mysoin Genes Expressed in Vertebrate Retina, Is Localized to the Calycal Processes of Rod and Cone Photoreceptors and Is Expressed in the Sacculus. A.C. Dose, D. Hillman, C. Wong, L. Sohlberg, J. Lin-Jones, and B. Burnside (2003) Mol. Biol. Cell 14:4173-4180.

A Class III Myosin Expressed in the Retina Is a Potential Candidate for Bardet-Biedl Syndrome. A.C. Dose and B. Burnside (2002) Genomics 79:621-624.

Cloning and Chromosomal Localization of a Human Class III Myosin. A.C. Dose and B. Burnside (2000) Genomics 67:333-342.

Novel Myosin VI Isoform is Abundantly Expressed in Retina. J. Breckler, K. Au, J. Cheng, T. Hasson, and B. Burnside (2000) Exp. Eye Res. 70:121-134.

Photoreceptor Localization of the KIF3A and KIF3B Subunits of the Heterotrimeric Microtuble Motor Kinesin II in Vertebrate Retina. J.L. Whitehead, S.Y. Wang, L. Bost-Usinger, E. Hoang, K.A. Frazer, and B. Burnside (1999) Exp. Eye Res. 69:491-503.

Characterization of a novel C-kinesin (KIFC3) abundantly expressed in vertebrate retina and RPE. E. Hoang, L. Bost-Usinger, and B. Burnside (1999) Exp. Eye Res. 69:57-68.

Last Updated 2008-09-15