Our laboratory utilizes fluorescence methodologies to elucidate dynamic aspects of biomolecules. We are currently studying dynamin, a large (98kDa) GTPase which functions to “pinch-off” membrane vesicles in pathways such as receptor mediated endocytosis and synaptic vesicle recycling. We carry out both in vitro and in vivo studies on the self-association modes of dynamin as well as its interaction with membranes and other proteins such as endophilin and Arc/Arg3.1. We have also been studying dynamins with mutations that cause motor disorders, specifically Centronuclear Myopathy and Charcot-Marie-Tooth disease. These studies, both in vitro and in living cells, are aimed at understanding the molecular basis for dynamin’s involvement in these disorders. Recently, we began a project to study, both in vitro and in vivo, the self-assembly of the protein Leucine Rich Repeat Kinase 2 or LRRK2. Mutations in the gene for LRRK2 are responsible for an autosomal dominant form of Parkinson’s Disease (PD). We also have a project on Botulinum Neurotoxin which involves biophysical studies on proteins forming the neurotoxin complex as well as development of in vitro and in vivo toxin assays based on Fluorescence Fluctuation Spectroscopy. Recently we have been developing the application of the phasor method, a visual approach to treatment of time-resolved fluorescence data, to in vitro systems such as intrinsic protein fluorescence.
Part of the ISS Chronus fluorescense lifetime instrument.
Monkey kidney cell line.