We have begun to structurally characterize myosin VIIa using NMR of purified protein domains. With Jim Seller's lab at the NIH, we used fast time course kinetics and single molecule assays to analyze molecular function and show that this myosin VIIa is a processive motor. We are beginning to characterize the proteins that collaborate with both myosin II and myosin VIIa using biochemical strategies in vitro, yeast two hybrid approaches in vivo and genetic interaction strategies in fly.
Drosophila with severe mutations in crinkled (ck), the gene that encodes MyoVIIa, display defects in hair and bristle morphology, suggesting ck/MyoVIIa is involved in the formation of actin-based structures. We are working to identify proteins and/or cargo that interact with ck/MyoVIIa and further examine the molecular mechanism behind ck/MyoVIIa’s role in the formation and maintenance of actin-based structures. In addition to hair and bristle formation, we are examining the morphology of actin-rich structures in early Drosophila development.
Drosophila ovaries fixed and stained for actin (left) and nuclei (right). Myosin VIIa is required for the normal development of ovaries in the fly.
