Neat!

Robert Molday

Professor
Ophthalmology and Visual Sciences
Director, Centre for Macular Research


Email: mol...@interchange.ubc.ca
Phone: 604 822-6173

Web pages: Lab webpage

Education

  • BSc (Honours-Chemistry), University of Pennsylvania, 1965
  • MSc (Chemistry), Georgetown University, 1967
  • PhD (Biochemistry), University of Pennsylvania, 1971
  • Postdoctoral Fellow: California Institute of Technology, 1975

Keywords

  • Vision
  • vertebrate retinal photoreceptor proteins
  • photoreceptor cell structure and morphogenesis
  • retinal cell-cell and cell-extracellular matrix interactions
  • inherited retinal degenerative diseases

Research Interests

Overview

Vision is the most important of our senses. It enables us to richly experience and interact with the world around us. Inherited diseases of the visual system that lead to partial or total blindness severely diminish the quality of life and present a serious social and economic burden.

Research in my laboratory is directed toward identifying and characterizing vertebrate retinal photoreceptor proteins and elucidating their role in 1) phototransduction and related signal transduction pathways; 2) photoreceptor cell structure and morphogenesis; 3) retinal cell-cell and cell-extracellular matrix interactions; and 4) various inherited retinal degenerative diseases including retinitis pigmentosa and macular degeneration that are the leading causes of blindness in the developed world. We are also developing and applying new technology to the study of membrane proteins and treatments for retinal degenerative diseases. To accomplish these goals, we are utilizing a variety of current and emerging biochemical, biophysical, immunochemical, molecular and cell biology approaches to 1) purify and reconstitute membrane proteins into lipid vesicles for structure-function analyses; 2) identify and characterize important structural, functional, and regulatory protein domains; 3) define specific protein-protein interactions responsible for the formation of macromolecular assemblies; 4) develop novel reagents and cell and animal models for analysis of retinal degenerative diseases; and 5) evaluate diagnostic and therapeutic interventions for selective retinal degenerative diseases.

Some of the techniques currently being employed in my laboratory include:

  • Generation and characterization of monoclonal antibodies
  • cDNA cloning, subcloning and sequencing
  • Heterologous protein expression in bacteria, yeast and mammalian cells
  • Construction of mutant and chimeric proteins using PCR
  • Yeast two hybrid analysis
  • Spectrophotometric analysis
  • Immunoaffinity and conventional column chromatographyp
  • HPLC peptide and FPLC protein chromatography
  • Proteomic analysis using mass spectroscopy
  • Peptide Synthesis
  • Immunoprecipitation and immunoaffinity chromatography
  • SDS gel electrophoresis and Western blotting
  • Immunocytochemical labeling for fluorescent light microscopy
  • Confocal scanning laser microscopy
  • Transmission and scanning electron microscopy
  • Enzyme and transport assays
  • Computer data analysis
  • Cell and subcellular fractionation
  • Cell and tissue culture techniques
  • Cell and tissue culture techniques
  • RNA extraction and Northern blotting
  • Analysis of transgenic and knockout animals
  • Gene therapy
  • Drug discovery

The experimental systems we work on and current research areas of interest are briefly described on this page.


Selected Publications

Wu, WW and Molday RS. (2003). Defective discoidin domain structure, subunit assembly, and endoplasmic reticulum processing of retinoschisin are primary mechanisms responsible for X-linked retinoschisis.J Biol Chem278:28139-46.

Loewen, CJ, Moritz OL, Tam BM, Papermaster DS, and Molday RS. (2003). The role of subunit assembly in peripherin-2 targeting to rod photoreceptor disk membranes and retinitis pigmentosaMol Biol Cell. 14:3400-13.

Ahn J., Beharry, S., Molday, L.L. and Molday, R.S. (2003). Functional interaction between the two halves of the photoreceptor-specific ATP binding cassette protein ABCR (ABCA4). Evidence for a non-exchangeable ADP in the first nucleotide binding domain.J. Biol. Chem., 278:39600-39608.

Weber, B.H.F., Schrewe, H., Molday, L.L., Gehrig, A., White, K., Seeliger, M.W, Jaissle, G.B., Friedburg, C., Tamm, T., and Molday, R.S. (2002) Inactivation of the murine X-linked juvenile retinoschisis gene, Rs1h, suggests a role of retinoschisin in retinal cell layer organization and synaptic structure.Proc. Natl. Acad. Sci. U.S.A. 99:6222-6227.

Zhong, H., Molday, L.L., Molday, R.S. and Yau, K-W. (2002) The Heteromeric Cyclic Nucleotide-gated Channel Adopts a 3A:1B stoichiometry.Nature420:193-198.

Warren, R. and Molday RS. (2002) Regulation of the rod photoreceptor cyclic nucleotide-gated channel.Adv Exp Med Biol. 514:205-23.

Poetsch, A., Molday, L.L. and Molday, R.S. (2001) The cGMP-gated Channel and Related Glutamic Acid Rich Proteins Interact with Peripherin-2 at the Rim Region of Rod Photoreceptor Disc Membranes.J. Biol. Chem. 276:48009-48016.

Bungert, S., Molday, L.L. and Molday, R.S. (2001) Membrane Topology of ABCR (ABCA4), ABC1 (ABCA1), and Related ABCA Transporters.J. Biol. Chem. 276:23539-23546

Loewen, C.J.R. and Molday, R.S. (2001) Molecular Characterization of Peripherin-2 and Rom-1 Mutants Responsible for Digneic Retinitis Pigmentosa.J. Biol. Chem. 276:22388-22396.

Molday, L.L., Sauer, C.G., Weber, B.H.F., and Molday, R.S. (2001) Molecular Characterization and Localization of RS1, the Protein Encoded by the Gene for X-linked Juvenile Retinoschisis.Invest. Ophthalmol. Vis. Sci. 42:816-825.

Molday, L.L., Rabin, A.R., and Molday, R.S. (2000) ABCR Expression in Foveal Cone photoreceptors and Its Role in Stargardt Macular Dystrophy.Nature Genetics25:257-258.

Other

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