Accelerated actin filament polymerization from microtubule plus ends.

Accelerated actin filament polymerization from microtubule plus ends.
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DOI:
10.1126/science.aaf1709
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发表时间:
2016-05-20
期刊:
Science (New York, N.Y.)
影响因子:
--
通讯作者:
Goode BL
Goode BL
中科院分区:
其他
文献类型:
--
作者:
Henty-Ridilla JL;Rankova A;Eskin JA;Kenny K;Goode BL

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Microtubules govern actin network remodeling in a wide range of biological processes, yet the mechanisms underlying this cytoskeletal crosstalk have remained obscure. Here we used single-molecule fluorescence microscopy to show that the microtubule plus-end associated protein CLIP-170 binds tightly to formins to accelerate actin filament elongation. Furthermore, we observed mDia1 dimers and CLIP-170 dimers co-tracking growing filament ends for minutes. CLIP-170-mDia1 complexes promoted actin polymerization approximately 18 times faster than free barbed end growth, while simultaneously enhancing protection from capping protein. We used a microtubule-actin dynamics co-reconstitution system to observe CLIP-170-mDia1 complexes being recruited to growing microtubule ends by EB1. The complexes triggered rapid growth of actin filaments that remained attached to the microtubule surface. These activities of CLIP-170 were required in primary neurons for normal dendritic morphology. Thus, our results reveal a cellular mechanism whereby growing microtubule plus-ends direct rapid actin assembly.
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