Abstract
Myosin-IXb (Myo9b) is a single-headed, processive motor1,2 that contains a Rho-GTPase-activating protein (GAP) domain within its tail3,4. Although tail-less myosin-IXb motor domain moves towards the minus end of the actin filament2, we show here that full-length myosin-IXb is a plus-end-directed motor. This suggests that the tail domain of myosin-IXb regulates motor directionality.
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Acknowledgements
We thank E. Osterweil for discussions and providing purified Rho, the Pollard laboratory for gel-filtered actin, W. Chang for Myo5a and M. J. Tyska for discussions. This work was supported by National Institutes of Health grants DK-25387 and DK 55389 and American Heart Association grant 9950204N.
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Supplementary Movie 1
Movement of a polarity-labeled filament by native Myo9b. Time lapse images show translocation of a filament with its plus end (labeled red) at the trailing end and minus end leading (green), demonstrating Myo9b is a plus-end-directed motor. Speed ~ 300X. Bar, 5 μm. (AVI 359 kb)
Supplementary Movie 1
Movement of a polarity-labeled filament by Myo5a. As for Myo9b, the red/plus end is trailing, indicating movement is plus-enddirected. Speed ~ 50X. Bar, 5 μm. (AVI 1971 kb)
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O'Connell, C., Mooseker, M. Native Myosin-IXb is a plus-, not a minus-end-directed motor. Nat Cell Biol 5, 171–172 (2003). https://doi.org/10.1038/ncb924
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DOI: https://doi.org/10.1038/ncb924
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