Evidence map›Paper›PMID 27199431›Full record

ArticleScience (New York, N.Y.)2016

Accelerated actin filament polymerization from microtubule plus ends.

Jessica L Henty-Ridilla, Aneliya Rankova, Julian A Eskin, Katelyn Kenny, Bruce L Goode

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.

0numbers the graph read from it
0cells of the map it votes in
105citing papers in PubMed
13.5field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

105 citing papers in PubMed, 189 citations in OpenAlex.

  1. Article
  2. Tubulin flux at spastin-induced nanodamage sites regulates microtubule rescue frequency and EB1 lifetimes.Proceedings of the National Academy of Sciences of the United States of America · 2026
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45 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Jessica L Henty-RidillaDepartment of Biology, Brandeis University, 415 South Street, Waltham, MA 02454, USA.
Aneliya RankovaDepartment of Biology, Brandeis University, 415 South Street, Waltham, MA 02454, USA.
Julian A EskinDepartment of Biology, Brandeis University, 415 South Street, Waltham, MA 02454, USA.
Katelyn KennyDepartment of Biology, Brandeis University, 415 South Street, Waltham, MA 02454, USA.
Bruce L GoodeDepartment of Biology, Brandeis University, 415 South Street, Waltham, MA 02454, USA. goode@brandeis.edu.
Brandeis University · US

Funding

Quantitative Neuroscience: Tools for Bridging Levels of AnalysisT32NS007292 · NINDS · BRANDEIS UNIVERSITY · PI GINA G TURRIGIANO · 1986 to 2026
$12.7M
Regulation of formins and cell polarity in yeastR01GM083137 · NIGMS · BRANDEIS UNIVERSITY · PI GOODE, BRUCE L · 2008 to 2019
$4.3M
Molecular Mechanisms coordinating the actin and microtubule cytoskeletonsR01GM098143 · NIGMS · BRANDEIS UNIVERSITY · PI GELLES, JEFF, GOODE, BRUCE L · 2012 to 2019
$2.6M
NIGMS NIH HHS GM083137NIGMS NIH HHS R01 GM083137NIGMS NIH HHS R01 GM098143NINDS NIH HHS T32 NS007292NINDS NIH HHS T32NS007292
6 · The paper itself

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.

Indexed as

Actin CytoskeletonAdaptor Proteins, Signal TransducingAnimalsCells, CulturedCytoskeletonFetal ProteinsForminsHumansMicrofilament ProteinsMicroscopy, FluorescenceMicrotubule-Associated ProteinsMicrotubulesNeoplasm ProteinsNeuronsNuclear ProteinsPolymerizationAdaptor Proteins, Signal Transducingcytoplasmic linker protein 170DIAPH1 protein, humanFetal ProteinsForminsMicrofilament ProteinsMicrotubule-Associated ProteinsNeoplasm ProteinsNuclear ProteinsProtein Isoforms

Identifiers

PMID27199431
PMCPMC5179141
OpenAlexW2402207766

What OpenQuestion holds

Textmetadata
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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.