Evidence map›Paper›PMID 35508487›Full record

ArticleNature communications2022

Cofilactin filaments regulate filopodial structure and dynamics in neuronal growth cones.

Ryan K Hylton, Jessica E Heebner, Michael A Grillo, Matthew T Swulius

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
6.0field-weighted citation impact, top 2% 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

28 citing papers in PubMed, 52 citations in OpenAlex.

  1. Myosin II-independent contraction of actin filaments in membrane nanotubes.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  15. Fascin structural plasticity mediates flexible actin bundle construction.bioRxiv : the preprint server for biology · 2024
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  17. Handling Difficult Cryo-ET Samples: A Study with Primary Neurons from Drosophila melanogaster.Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada · 2023
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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

4 authors at 1 institution in 1 country.

Ryan K HyltonDepartment of Biochemistry and Molecular Biology, Penn State College of Medicine, Hershey, PA, USA.ORCID 0000-0002-1549-8521
Jessica E HeebnerDepartment of Biochemistry and Molecular Biology, Penn State College of Medicine, Hershey, PA, USA.
Michael A GrilloDepartment of Biochemistry and Molecular Biology, Penn State College of Medicine, Hershey, PA, USA.
Matthew T SwuliusDepartment of Biochemistry and Molecular Biology, Penn State College of Medicine, Hershey, PA, USA. mts286@psu.edu.ORCID 0000-0002-8147-208X
Penn State Milton S. Hershey Medical Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cofilin is best known for its ability to sever actin filaments and facilitate cytoskeletal recycling inside of cells, but at higher concentrations in vitro, cofilin stabilizes a more flexible, hyper-twisted state of actin known as "cofilactin". While this filament state is well studied, a structural role for cofilactin in dynamic cellular processes has not been observed. With a combination of cryo-electron tomography and fluorescence imaging in neuronal growth cones, we observe that filopodial actin filaments switch between a fascin-linked and a cofilin-decorated state, and that cofilactin is associated with a variety of dynamic events within filopodia. The switch to cofilactin filaments occurs in a graded fashion and correlates with a decline in fascin cross-linking within the filopodia, which is associated with curvature in the bundle. Our tomographic data reveal that the hyper-twisting of actin from cofilin binding leads to a rearrangement of filament packing, which largely excludes fascin from the base of filopodia. Our results provide mechanistic insight into the fundamentals of cytoskeletal remodeling inside of confined cellular spaces, and how the interplay between fascin and cofilin regulates the dynamics of searching filopodia.

Indexed as

ActinsPseudopodiaActin CytoskeletonActin Depolymerizing FactorsGrowth ConesActin Depolymerizing FactorsActins

Identifiers

PMID35508487
PMCPMC9068697
OpenAlexW4225376724

What OpenQuestion holds

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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.