The mitotic kinesin-14 KlpA contains a context-dependent directionality switch.
The mitotic kinesin-14 KlpA contains a context-dependent directionality switch.
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DOI:
10.1038/ncomms13999
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发表时间:
2017-01-04
影响因子:
16.6
通讯作者:
中科院分区:
文献类型:
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Kinesin-14s are commonly known as nonprocessive minus end-directed microtubule motors that function mainly for mitotic spindle assembly. Here we show using total internal reflection fluorescence microscopy that KlpA—a kinesin-14 from Aspergillus nidulans—is a context-dependent bidirectional motor. KlpA exhibits plus end-directed processive motility on single microtubules, but reverts to canonical minus end-directed motility when anchored on the surface in microtubule-gliding experiments or interacting with a pair of microtubules in microtubule-sliding experiments. Plus end-directed processive motility of KlpA on single microtubules depends on its N-terminal nonmotor microtubule-binding tail, as KlpA without the tail is nonprocessive and minus end-directed. We suggest that the tail is a de facto directionality switch for KlpA motility: when the tail binds to the same microtubule as the motor domain, KlpA is a plus end-directed processive motor; in contrast, when the tail detaches from the microtubule to which the motor domain binds, KlpA becomes minus end-directed. Kinesin-14s are commonly considered to be minus end-directed microtubule motor proteins. Here the authors show that KlpA, a fungal kinesin-14 orthologue, relies on its N-terminal nonmotor microtubule-binding tail to achieve context-dependent bidirectional motility.
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影响因子:
64.5
作者:
Case, RB;Pierce, DW;Vale, RD
通讯作者:
Vale, RD
DOI:
10.1083/jcb.152.3.425
发表时间:
2001-02-05
期刊:
The Journal of cell biology
影响因子:
--
作者:
Gordon MB;Howard L;Compton DA
通讯作者:
Compton DA
影响因子:
11.6
作者:
Ambrose, J. Christian;Cyr, Richard
通讯作者:
Cyr, Richard
影响因子:
16.6
作者:
Chavali PL;Chandrasekaran G;Barr AR;Tátrai P;Taylor C;Papachristou EK;Woods CG;Chavali S;Gergely F
通讯作者:
Gergely F
影响因子:
21.3
作者:
Fink, Gero;Hajdo, Lukasz;Diez, Stefan
通讯作者:
Diez, Stefan