Abstract
Microtubules (MTs) interact with force-generating proteins to generate a variety of intracellular movements, including intracellular particle transport, ciliary–flagellar beating, and chromosome–spindle movements during mitosis–meiosis. Relatively little is known about the mechanics of these motor-MT interactions, in part because the motor binding domains of the MT and the corresponding MT binding domains of the motor have not been well characterized. Using a flagellar motility assay, we report that the MT subunits, α- and β-tubulin, each contain a dynein binding domain located near the C-termini of their respective tubulin subunits. Blocking either α- or β-tubulin binding domains of dynein attenuates motility in demembranated sea urchin sperm up to 50%. Interestingly, blocking both α- and β-tubulin binding domains on dynein produces much greater decreases in motility. These data suggest that flagellar dynein binds to both subunits of the MT polymer, α- and β-tubulin. In addition, the two subunits appear to contribute equivalent, but functionally separate, roles to flagellar motility.Key words: microtubule, microtubule-based motility, dynein, sperm motility.
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Dates
Type | When |
---|---|
Created | 14 years, 4 months ago (April 22, 2011, 9:49 p.m.) |
Deposited | 1 month, 3 weeks ago (July 2, 2025, 2:21 p.m.) |
Indexed | 1 month, 3 weeks ago (July 2, 2025, 2:40 p.m.) |
Issued | 29 years, 11 months ago (Sept. 1, 1995) |
Published | 29 years, 11 months ago (Sept. 1, 1995) |
Published Print | 29 years, 11 months ago (Sept. 1, 1995) |
@article{Goldsmith_1995, title={Mechanics of motility: distinct dynein binding domains on α- and β-tubulin}, volume={73}, ISSN={1208-6002}, url={http://dx.doi.org/10.1139/o95-074}, DOI={10.1139/o95-074}, number={9–10}, journal={Biochemistry and Cell Biology}, publisher={Canadian Science Publishing}, author={Goldsmith, Matthew and Kooy, Derek van der and Yarbrough, Lynwood}, year={1995}, month=sep, pages={665–671} }