Photoreceptor Protein Dynamics, Transport and Localization
The Calvert lab studies the dynamics of proteins in live retinal photoreceptors and other ciliated cells to determine how they are transported to and localized within subcellular compartments.
His lab has developed novel, quantitative tools that are being used to probe the dynamics of specific proteins within the living cells in which they normally reside and to determine how mutations that lead to disease cause the proteins to misbehave. Integral to this approach is the use of multiphoton and confocal optical methods to image molecules within living cells from transgenic animals, or from cell culture, that express proteins fused to fluorescent tags. Investigating the dynamics of normal proteins within cells and how they change when mutated will lead to a better understanding of the mechanisms underlying devastating blinding diseases, such as retinitis pigmentosa, as well as other ciliopathies, and may ultimately lead to new therapeutic strategies.
Dr. Calvert’s work is published in the Journal of General Physiology, the Journal of Microscopy, Nature, Science, the Proceedings of the National Academy of Sciences, the Journal of Neuroscience, the Journal of Cell Science, the Journal of Biological Chemistry, Molecular Vision, Trends in Cell Biology, and Investigative Ophthalmology and Visual Science. He has authored three review articles and book chapters.
Dr. Calvert is recipient of a Career Development Award from Research to Prevent Blindness and a Vision Research Grant from the Karl Kirchgessner Foundation. His work is supported by a grant from the National Eye Institute of the National Institutes of health (NIH). As a postdoctoral fellow he received an Individual National Research Service Award from the National Institutes of Health. He collaborates with researchers from the University of California - Davis, Lehigh University and Duke University. He is a regular referee for the Journal of Neuroscience, the Journal of General Physiology, and the Journal of Biological Chemistry and has been invited to critique applications for grants from the Welcome Trust and the NATO Human Frontier Science program.