Molecular Evolution of MyTH-FERM Myosin Motor Proteins
Myosins are a highly diverse family of actin-based motor proteins present in almost every eukaryote. The MyTH4-FERM myosins are found at the tips of parallel actin bundles and are involved in diverse functions including cell migration, phagocytosis, and sensory perception. The vertebrate MF myosins 7, 10 and 15 have roles in regulating the growth of parallel actin bundles such as filopodia (Myo10) and stereocilia (Myo7, Myo15), as does the Myo7-like MF myosin that is essential for filopod extension in the amoeba Dictyostelium. The similar localization and functions of the amoeba and the vertebrate MF myosins as well as the conservation of tail domain sequences suggest that the amoeba myosins could be useful models for the vertebrate MF myosins.
These researchers seek to understand the molecular evolution of MF myosins using a sequence-based approach. They focus on two structural domains: the motor domain and the FERM domain, a globular domain that often interacts with membranes or membrane proteins. This two-domain approach uncovers similarities between myosin sequences with divergent tail regions and tests whether unconventional myosins share a common molecular ancestor with a conserved set of structural domains. Recent results from imaging work suggest that MF myosins share common mechanisms of regulation at conserved residues. This project will guide the researchers as they investigate how new myosin functions may have evolved.
A bibliography of this group’s publications is attached.
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