A Nonprocessive Class V Myosin Drives Cargo Processively When a Kinesin- Related Protein Is a Passenger

During secretory events, kinesin transports cargo along microtubules and then shifts control to myosin V for delivery on actin filaments to the cell membrane [1]. When kinesin and myosin V are present on the same cargo, kinesin interacts electrostatically with actin to enhance myosin V-based transpo...

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Bibliographic Details
Published in:Current biology 2009-12, Vol.19 (24), p.2121-2125
Main Authors: Hodges, Alex R., Bookwalter, Carol S., Krementsova, Elena B., Trybus, Kathleen M.
Format: Article
Language:English
Subjects:
Actins - metabolism
Binding, Competitive - physiology
Biological Transport - physiology
Carrier Proteins - metabolism
CELLBIO
Electrophoresis, Polyacrylamide Gel
Microscopy, Fluorescence
Microtubule-Associated Proteins - metabolism
Models, Molecular
Myosin Heavy Chains - metabolism
Myosin Type V - metabolism
Quantum Dots
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins - metabolism
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Summary:During secretory events, kinesin transports cargo along microtubules and then shifts control to myosin V for delivery on actin filaments to the cell membrane [1]. When kinesin and myosin V are present on the same cargo, kinesin interacts electrostatically with actin to enhance myosin V-based transport in vitro [2]. The relevance of this observation within the cell was questioned. In budding yeast, overexpression of a kinesin-family protein (Smy1p) suppressed a transport defect in a strain with a mutant class V myosin (Myo2p) [3]. We postulate that this is a cellular manifestation of the in vitro observation. We demonstrate that Smy1p binds electrostatically to actin bundles. Although a single Myo2p cannot transport cargo along actin bundles, addition of Smy1p causes the complex to undergo long-range, continuous movement. We propose that the kinesin-family protein acts as a tether that prevents cargo dissociation from actin, allowing the myosin to take many steps before dissociating. We demonstrate that both the tether and the motor reside on moving secretory vesicles in yeast cells, a necessary feature for this mechanism to apply in vivo. The presence of both kinesin and myosin on the same cargo may be a general mechanism to enhance cellular transport in yeast and higher organisms.
ISSN:0960-9822
1879-0445
DOI:10.1016/j.cub.2009.10.069