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• W2022276471 endingPage "3131" @default.
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• W2022276471 abstract "Myosin V is a single-molecule motor that moves organelles along actin. When myosin V pulls loads inside the cell in a highly viscous environment, the force on the motor is unlikely to be constant. We propose that the tether between the single-molecule motor and the cargo (i.e., the extended tail domain of the molecule) must be able to absorb the sudden mechanical motions of the motor and allow smooth relaxation of the motion of the cargo to a new position. To test this hypothesis, we compared the elastic properties of the extended tail domains of processive (mouse myosin Va) and nonprocessive (Drosophila myosin V) molecular motors. The extended tail domain of these myosins consists of mechanically strong coiled-coil regions interspersed with flexible loops. In this work we explored the mechanical properties of coiled-coil regions using atomic force microscopy. We found that the processive and nonprocessive coiled-coil fragments display different unfolding patterns. The unfolding of coiled-coil structures occurs much later during the atomic force microscopy stretch cycle for processive myosin Va than for nonprocessive Drosophila myosin V, suggesting that this elastic tether between the cargo and motor may play an important role in sustaining the processive motions of this single-molecule motor." @default.
• W2022276471 created "2016-06-24" @default.
• W2022276471 creator A5043012356 @default.
• W2022276471 creator A5073264020 @default.
• W2022276471 creator A5090482118 @default.
• W2022276471 date "2009-12-01" @default.
• W2022276471 modified "2023-09-28" @default.
• W2022276471 title "Extensibility of the Extended Tail Domain of Processive and Nonprocessive Myosin V Molecules" @default.
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• W2022276471 doi "https://doi.org/10.1016/j.bpj.2009.09.033" @default.
• W2022276471 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2793355" @default.
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