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- W3105757968 abstract "Abstract The regulation of actin dynamics is essential for various cellular processes. Former evidence suggests a correlation between the function of non-conventional myosin motors and actin dynamics. We investigate the contribution of myosin1b to actin dynamics using sliding motility assays. We observe that sliding on myosin1b immobilized or bound to a fluid bilayer enhances actin depolymerization at the barbed end, while sliding on myosin II, although 5 times faster, has no effect. This work reveals a non-conventional myosin motor as a new type of depolymerase and points to its singular interactions with the actin barbed end." @default.
- W3105757968 created "2020-11-23" @default.
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- W3105757968 date "2018-07-24" @default.
- W3105757968 modified "2023-10-18" @default.
- W3105757968 title "A new actin depolymerase: a Myosin 1 motor" @default.
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- W3105757968 doi "https://doi.org/10.1101/375923" @default.
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