Key result
Ensembles of membrane-bound Myo1c can generate and sustain sub-piconewton forces parallel to fluid lipid bilayers, with larger forces achieved when working away from the membrane plane or anchored to slowly diffusing regions.
Membrane-bound Myo1c ensembles can generate forces parallel to lipid bilayers, which is enhanced when working away from the membrane plane or anchored to slowly diffusing regions.
Vertebrate myosin-IC (Myo1c) is a type-1 myosin that links cell membranes to the cytoskeleton via its actin-binding motor domain and its phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2)-binding tail domain. While it is known that Myo1c bound to PtdIns(4,5)P2 in fluid-lipid bilayers can propel actin filaments in an unloaded motility assay, its ability to develop forces against external load on actin while bound to fluid bilayers has not been explored. Using optical tweezers, we measured the diffusion coefficient of single membrane-bound Myo1c molecules by force-relaxation experiments, and the ability of ensembles of membrane-bound Myo1c molecules to develop and sustain forces. To interpret our results, we developed a computational model that recapitulates the basic features of our experimental ensemble data and suggests that Myo1c ensembles can generate forces parallel to lipid bilayers, with larger forces achieved when the myosin works away from the plane of the membrane or when anchored to slowly diffusing regions.
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Pyrpassopoulos et al. (2016) studied this question. Membrane-associated Myo1c was evaluated on Force generation and diffusion coefficient of membrane-bound Myo1c. Ensembles of membrane-bound Myo1c can generate and sustain sub-piconewton forces parallel to fluid lipid bilayers, with larger forces achieved when working away from the membrane plane or anchored to slowly diffusing regions.
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