title: Leveraging the membrane - cytoskeleton interface with myosin-1.
abstract: Class 1 myosins are small motor proteins with the ability to simultaneously bind to actin filaments and cellular membranes. Given their ability to generate mechanical force, and their high prevalence in many cell types, these molecules are well positioned to carry out several important biological functions at the interface of membrane and the actin cytoskeleton. Indeed, recent studies implicate these motors in endocytosis, exocytosis, release of extracellular vesicles, and the regulation of tension between membrane and the cytoskeleton. Many class 1 myosins also exhibit a load-dependent mechano-chemical cycle that enables them to maintain tension for long periods of time without hydrolyzing ATP. These properties put myosins-1 in a unique position to regulate dynamic membrane-cytoskeleton interactions and respond to physical forces during these events.
authors.affiliation: Department of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, TN 37205, USA.
authors.forename: Russell E
authors.initials: RE
authors.lastname: McConnell
authors.forename: Matthew J
authors.initials: MJ
authors.lastname: Tyska
mesh_terms: D000048:Acanthamoeba / Q000166:cytology; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D003599:Cytoskeleton / Q000378:metabolism*; D004023:Dictyostelium / Q000166:cytology; D004705:Endocytosis; D005089:Exocytosis; D006801:Humans; D008958:Models, Molecular; D024461:Myosin Type I / Q000378:metabolism*
chemical_list: D000255:Adenosine Triphosphate; D024461:Myosin Type I
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