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Control of cytoplasmic dynein force production and processivity by its C-terminal domain.

Nature communications | 2015

Cytoplasmic dynein is a microtubule motor involved in cargo transport, nuclear migration and cell division. Despite structural conservation of the dynein motor domain from yeast to higher eukaryotes, the extensively studied S. cerevisiae dynein behaves distinctly from mammalian dyneins, which produce far less force and travel over shorter distances. However, isolated reports of yeast-like force production by mammalian dynein have called interspecies differences into question. We report that functional differences between yeast and mammalian dynein are real and attributable to a C-terminal motor element absent in yeast, which resembles a 'cap' over the central pore of the mammalian dynein motor domain. Removal of this cap increases the force generation of rat dynein from 1 pN to a yeast-like 6 pN and greatly increases its travel distance. Our findings identify the CT-cap as a novel regulator of dynein function.

Pubmed ID: 25670086 RIS Download

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Associated grants

  • Agency: NIGMS NIH HHS, United States
    Id: R01 GM098469
  • Agency: NIDDK NIH HHS, United States
    Id: P30 DK041296
  • Agency: NIGMS NIH HHS, United States
    Id: GM102347
  • Agency: NIGMS NIH HHS, United States
    Id: R01 GM094415
  • Agency: NIGMS NIH HHS, United States
    Id: T32GM007288
  • Agency: NIGMS NIH HHS, United States
    Id: T32 GM007288
  • Agency: NIGMS NIH HHS, United States
    Id: GM094415
  • Agency: NIGMS NIH HHS, United States
    Id: R01 GM102347

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