Evidence map›Paper›PMID 30601697›Full record

ArticleMolecular biology of the cell2019

Ena/VASP processive elongation is modulated by avidity on actin filaments bundled by the filopodia cross-linker fascin.

Alyssa J Harker, Harshwardhan H Katkar, Tamara C Bidone, Fikret Aydin, Gregory A Voth, Derek A Applewhite, David R Kovar

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

34 citing papers in PubMed, 63 citations in OpenAlex.

  1. Review
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  4. Molecular mechanism of Arp2/3 complex activation by nucleation-promoting factors and an actin monomer.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  14. Review
  15. Biochemical and mechanical regulation of actin dynamics.Nature reviews. Molecular cell biology · 2022
    Review
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  18. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 1 country.

Alyssa J HarkerDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637.
Harshwardhan H KatkarDepartment of Chemistry, cThe James Franck Institute, and dInstitute for Biophysical Dynamics, University of Chicago, Chicago, IL 60637.
Tamara C BidoneDepartment of Chemistry, cThe James Franck Institute, and dInstitute for Biophysical Dynamics, University of Chicago, Chicago, IL 60637.
Fikret AydinDepartment of Chemistry, cThe James Franck Institute, and dInstitute for Biophysical Dynamics, University of Chicago, Chicago, IL 60637.
Gregory A VothDepartment of Chemistry, cThe James Franck Institute, and dInstitute for Biophysical Dynamics, University of Chicago, Chicago, IL 60637.
Derek A ApplewhiteDepartment of Biology, Reed College, Portland, OR 97202.
David R KovarDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637.
Chicago Institute for Psychoanalysis · USUniversity of Chicago · USReed College · US

Funding

Molecular And Cellular Biology Training ProgramT32GM007183 · NIGMS · UNIVERSITY OF CHICAGO · PI GLICK, BENJAMIN S, RICE, PHOEBE A · 1985 to 2021
$23.9M
DROSOPHILA GENOMICS RESOURCE CENTERP40OD010949 · OD · TRUSTEES OF INDIANA UNIVERSITY · PI Andrew Zelhof · 2012 to 2026
$9.4M
Mechanisms of Formin-Mediated Actin Filament Assembly - Renewal 01 - ResubmissionR01GM079265 · NIGMS · UNIVERSITY OF CHICAGO · PI KOVAR, DAVID R · 2007 to 2023
$4.5M
National Science Foundation DMR-1420709NIGMS NIH HHS R01 GM079265NIGMS NIH HHS T32 GM007183NIH HHS P40 OD010949
6 · The paper itself

Abstract

Ena/VASP tetramers are processive actin elongation factors that localize to diverse F-actin networks composed of filaments bundled by different cross-linking proteins, such as filopodia (fascin), lamellipodia (fimbrin), and stress fibers (α-actinin). Previously, we found that Ena takes approximately threefold longer processive runs on trailing barbed ends of fascin-bundled F-actin. Here, we used single-molecule TIRFM (total internal reflection fluorescence microscopy) and developed a kinetic model to further dissect Ena/VASP's processive mechanism on bundled filaments. We discovered that Ena's enhanced processivity on trailing barbed ends is specific to fascin bundles, with no enhancement on fimbrin or α-actinin bundles. Notably, Ena/VASP's processive run length increases with the number of both fascin-bundled filaments and Ena "arms," revealing avidity facilitates enhanced processivity. Consistently, Ena tetramers form more filopodia than mutant dimer and trimers in Drosophila culture cells. Moreover, enhanced processivity on trailing barbed ends of fascin-bundled filaments is an evolutionarily conserved property of Ena/VASP homologues, including human VASP and Caenorhabditis elegans UNC-34. These results demonstrate that Ena tetramers are tailored for enhanced processivity on fascin bundles and that avidity of multiple arms associating with multiple filaments is critical for this process. Furthermore, we discovered a novel regulatory process whereby bundle size and bundling protein specificity control activities of a processive assembly factor.

Indexed as

Actin CytoskeletonActininActinsAnimalsCarrier ProteinsCell LineCytoskeletal ProteinsCytoskeletonKineticsMiceMicrofilament ProteinsMicroscopy, FluorescencePeptide Chain Elongation, TranslationalProtein BindingPseudopodiaActininActinsCarrier ProteinsCytoskeletal ProteinsEnah protein, mousefascinMicrofilament Proteins

Identifiers

PMID30601697
PMCPMC6589784
OpenAlexW2950120871

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.