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Melanosomes are localized with nanometer resolution inside cells and tracked as they move along microtubules and actin filaments. Single 8 nm steps powered by kinesin or dynein are observed for anterograde or retrograde movements along microtubules, with myosinV-powered 35 nm steps observed along actin filaments. Interestingly, a single melanasome was observed switching between microtubule and actin tracks as inferred from changes in direction that correlate with a change in step size.
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Kural C., Serpinskaya A.S., Chou Y.H., Goldman R.D., Gelfand V.I., and Selvin P.R. Tracking melanosomes inside a cell to study molecular motors and their interaction. Proc Natl Acad Sci U S A 104 (2007) 5378-5382. Melanosomes are localized with nanometer resolution inside cells and tracked as they move along microtubules and actin filaments. Single 8 nm steps powered by kinesin or dynein are observed for anterograde or retrograde movements along microtubules, with myosinV-powered 35 nm steps observed along actin filaments. Interestingly, a single melanasome was observed switching between microtubule and actin tracks as inferred from changes in direction that correlate with a change in step size.
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GFP-tagged peroxisomes were tracked as they moved bidirectionally on microtubules in S2 cells. The authors proposed that multiple kinesin and dynein may work together to generate cargo speeds 10 times that of speeds measured in vitro.
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Anti-HER2 antibody-labeled quantum dots (Qdots) were endocytosed into breast cancer cells. The Qdot-containing vesicles were observed while being transported by myosin VI lying just beneath the cell membrane, then switching to microtubules to be transported by dynein toward the cell nucleus.
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Each myosin V head was labeled with a different color Qdot, demonstrating directly that the heads move in a hand-over-hand manner, with each head taking 72 nm steps.
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In vitro study of beads trafficked by one, two, or multiple kinesin motors along tau-coated microtubules. Tau blocks kinesin binding altering the behavior of kinesin-coated beads at microtubule intersections.
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First characterization of the Eg5 kinesin motor's velocity and stepping under various loading conditions and ATP concentration. A three-state biochemical model is shown to explain Eg5's stepping kinetics.
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Qdot-labeled myosin V maneuvers through actin-actin intersections by switching between filaments or crossing over. Remarkably, myosin V molecules were observed diffusing on microtubules by an electrostatic mechanism that may be an important component associated with intracellular cargo transport.
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