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Project abstract for group titusmeg
Molecular Evolution of MyTH-FERM Myosins
Myosin is a highly conserved motor protein in eukaryotes that provides the force for directed cell motility, helps to control cell shape and transports cargo within cells. The best known myosin, Myosin 2, generates force in muscle. Myosin contains a motor domain and a tail domain. The variable structure of the tail reflects a huge diversity of myosin with at least 48 distinct classes identified to date. One subgroup of myosins, the MyTH-FERM myosins, is conserved across species from amoebas to humans. MyTH-FERM myosins are needed for vision, hearing, and neural development in humans, while MyTH-FERM myosins are important for cell adhesion and chemotaxis in amoebas. All MyTH-FERM myosins localize to the tips of parallel actin bundles, between actin and the cell membrane, in structures called filopodia and stereocilia. This finding, combined with the affinity of the MyTH-FERM domains for cytoskeletal proteins, suggests that MyTH-FERM myosins may have evolutionarily conserved functions in linking the cytoskeleton to the cell membrane. This project seeks to test this hypothesis using publicly available software to perform multiple sequence alignments and phylogenetic analysis of myosin protein sequences from an international database. Understanding the evolution of MyTH-FERM myosins will lead to new insights into their roles in cell adhesion, cell motility, and development.
A bibliography of this group’s publications acknowledging MSI is attached.