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Science. 2016 May 20;352(6288):1004-9. doi: 10.1126/science.aaf1709.

Accelerated actin filament polymerization from microtubule plus ends.

Author information

1
Department of Biology, Brandeis University, 415 South Street, Waltham, MA 02454, USA.
2
Department of Biology, Brandeis University, 415 South Street, Waltham, MA 02454, USA. goode@brandeis.edu.

Abstract

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

PMID:
27199431
PMCID:
PMC5179141
DOI:
10.1126/science.aaf1709
[Indexed for MEDLINE]
Free PMC Article

Conflict of interest statement

The authors declare no conflict of interest. Supplementary materials contain additional data.

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