Abstract
The single-headed myosins called myosin-I were first isolated from the protozoan Acanthamoeba and subsequently identified in other cells. We previously reported evidence that myosin-I is responsible for the movement of membranes, extracted from Acanthamoeba, along actin filaments in vitro. Here we show for the first time that myosin-I can bind directly to NaOH-extracted membranes isolated from Acanthamoeba and to vesicles of pure lipids with an affinity sufficient for extensive binding in the cell. Membrane-bound myosin-I may provide a mechanism for many cellular movements previously thought to involve filamentous myosin-II.
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