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

Control of cytoplasmic dynein force production and processivity by its C-terminal domain.
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DOI:
10.1038/ncomms7206
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发表时间:
2015-02-11
影响因子:
16.6
通讯作者:
Gennerich, Arne
Gennerich, Arne
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Nicholas, Matthew P.;Hoeoek, Peter;Brenner, Sibylle;Wynne, Caitlin L.;Vallee, Richard B.;Gennerich, Arne

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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. Cytoplasmic dynein from the yeast S. cerevisiae behaves distinctly from mammalian dyneins, despite structural conservation. Here, Nicholas et al. identify a C-terminal domain in mammalian dynein that restricts force generation and travel distance, which, when removed, allows mammalian dynein to behave like its yeast counterpart.
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