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- W2071070576 abstract "Myosin VI, the only known minus-ended actin filament-dependent motor, plays diverse cellular roles both as a processive motor and as a mechanical anchor. Although myosin VI has a short lever arm containing only one IQ-motif and a unique insertion for CaM binding, the motor walks with large and variable step sizes of ∼30-36 nm. Here, we show that the previously predicted coiled-coil domain immediately following the IQ-motifs (referred to as the lever arm extension (LAE)) adopts a stable monomeric, three-helix bundle fold in solution. Importantly, the LAE can undergo reversible, lipid membrane-dependent conformational changes. Upon exposure to lipid membranes, the LAE adopts a partially extended rod shape, and the removal of lipids from the LAE converts it back into the compact helix bundle structure. Molecular dynamics simulations indicate that lipid membrane binding may initiate unfolding and thereby trigger the LAE expansion. This reversible, lipid membrane-dependent expansion of the LAE provides a mechanistic base for myosin VI to walk with large and variable step sizes." @default.
- W2071070576 created "2016-06-24" @default.
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- W2071070576 date "2012-10-01" @default.
- W2071070576 modified "2023-10-14" @default.
- W2071070576 title "Membrane-induced Lever Arm Expansion Allows Myosin VI to Walk with Large and Variable Step Sizes" @default.
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- W2071070576 doi "https://doi.org/10.1074/jbc.m111.328781" @default.
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