Evidence map›Paper›PMID 32579429›Full record

ArticleMolecular biology of the cell2020

Initiation and disassembly of filopodia tip complexes containing VASP and lamellipodin.

Karen W Cheng, R Dyche Mullins

Open access · bronzeAbstract read
In one paragraph

Article in Molecular biology of the cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

27 citing papers in PubMed, 52 citations in OpenAlex.

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  13. Liquid-like condensates mediate competition between actin branching and bundling.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Article
  15. Chiral growth of adherent filopodia.Biophysical journal · 2023
    Article
  16. Article
  17. Article
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  19. Biochemical and mechanical regulation of actin dynamics.Nature reviews. Molecular cell biology · 2022
    Review
  20. Article
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

2 authors at 2 institutions in 1 country.

Karen W ChengDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143.
R Dyche MullinsDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143.
Howard Hughes Medical Institute · USUniversity of California, San Francisco · US

Funding

Assembly and function of cytoskeletal systems in eukaryotic and prokaryoticcellsR35GM118119 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MULLINS, R DYCHE · 2016 to 2025
$4.8M
Howard Hughes Medical InstituteNIGMS NIH HHS R35 GM118119
6 · The paper itself

Abstract

The shapes of many eukaryotic cells depends on the actin cytoskeleton, and changes in actin assembly dynamics underlie many changes in cell shape. Ena/VASP-family actin polymerases, for example, modulate cell shape by accelerating actin filament assembly locally and slowing filament capping. When concentrated into discrete foci at the leading edge, VASP promotes filopodia assembly and forms part of a poorly understood molecular complex that remains associated with growing filopodia tips. Here we identify precursors of this filopodia tip complex in migrating B16F1 cells: small leading-edge clusters of the adaptor protein lamellipodin (Lpd) that subsequently recruit VASP and initiate filopodia formation. Dimerization, membrane association, and VASP binding are all required for lamellipodin to incorporate into filopodia tip complexes, and overexpression of monomeric, membrane--targeted lamellipodin mutants disrupts tip complex assembly. Once formed, tip complexes containing VASP and lamellipodin grow by fusing with each other, but their growth is limited by a size-dependent dynamic instability. Our results demonstrate that assembly and disassembly dynamics of filopodia tip complexes are determined, in part, by a network of multivalent interactions between Ena/VASP proteins, EVH1 ligands, and actin filaments.

Indexed as

Actin CytoskeletonActinsAnimalsCarrier ProteinsCell Adhesion MoleculesCell LineCell MovementCell ShapeCytoskeletonDNA-Binding ProteinsMembrane ProteinsMiceMicrofilament ProteinsPhosphoproteinsPhosphorylationPseudopodiaActinsCarrier ProteinsCell Adhesion MoleculesDNA-Binding ProteinsENA-VASP proteinsMembrane ProteinsMicrofilament ProteinsPhosphoproteinsRaph1 protein, mouseVasodilator-Stimulated Phosphoprotein

Identifiers

PMID32579429
PMCPMC7543071
OpenAlexW3037074917

What OpenQuestion holds

Textmetadata
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.