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Curr Biol. 2009 Feb 10;19(3):196-205. doi: 10.1016/j.cub.2008.12.047. Epub 2009 Jan 29.

Motor- and tail-dependent targeting of dynein to microtubule plus ends and the cell cortex.

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Biology Department, University of Massachusetts at Amherst, Amherst, MA 01003, USA.



Cytoplasmic dynein mediates spindle positioning in budding yeast by powering sliding of microtubules along the cell cortex. Although previous studies have demonstrated cortical and plus-end targeting of dynein heavy chain (Dyn1/HC), the regulation of its recruitment to these sites remains elusive.


Here we show that separate domains of Dyn1/HC confer differential localization to the dynein complex. The N-terminal tail domain targets Dyn1/HC to cortical Num1 receptor sites, whereas the C-terminal motor domain targets Dyn1/HC to microtubule plus ends in a Bik1/CLIP-170- and Pac1/LIS1-dependent manner. Surprisingly, the isolated motor domain blocks plus-end targeting of Dyn1/HC, leading to a dominant-negative effect on dynein function. Overexpression of Pac1/LIS1, but not Bik1/CLIP-170, rescues the dominant negativity by restoring Dyn1/HC to plus ends. In contrast, the isolated tail domain has no inhibitory effect on Dyn1/HC targeting and function. However, cortical targeting of the tail construct is more robust than full-length Dyn1/HC and occurs independently of Bik1/CLIP-170 or Pac1/LIS1.


Our results suggest that the cortical association domain is normally masked in the full-length dynein molecule. We propose that targeting of dynein to plus ends unmasks the tail, priming the motor for off-loading to cortical Num1 sites.

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