Evidence map›Paper›PMID 30470968›Full record

ReviewBiophysical reviews2018

From solution to surface to filament: actin flux into branched networks.

R Dyche Mullins, Peter Bieling, Daniel A Fletcher

Open access · greenAbstract readReview
In one paragraph

Review in Biophysical reviews, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

31 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
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  8. The role of actin cytoskeleton component Arp2/3 in inflammatory response.Frontiers in cell and developmental biology · 2025
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Polymerization force-regulated actin filament-Arp2/3 complex interaction dominates self-adaptive cell migrations.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  15. Article
  16. Article
  17. Article
  18. Structure of Arp2/3 complex at a branched actin filament junction resolved by single-particle cryo-electron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  19. 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

3 authors at 3 institutions in 2 countries.

R Dyche MullinsHoward Hughes Medical Institute and Department of Cellular and Molecular Pharmacology, UCSF School of Medicine, San Francisco, CA, USA. dyche.mullins@ucsf.edu.ORCID http://orcid.org/0000-0002-0871-5479
Peter BielingMax Planck Institute of Molecular Physiology, Dortmund, Germany.
Daniel A FletcherDepartment of Bioengineering, University of California, Berkeley, CA, USA.
Howard Hughes Medical Institute · USMax Planck Institute of Molecular Physiology · DEUniversity of California, Berkeley · 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 Institute n/aNational Institute of General Medical Sciences R35 GM118119-03NIGMS NIH HHS R35 GM118119
6 · The paper itself

Abstract

The actin cytoskeleton comprises a set of filament networks that perform essential functions in eukaryotic cells. The idea that actin filaments incorporate monomers directly from solution forms both the "textbook picture" of filament elongation and a conventional starting point for quantitative modeling of cellular actin dynamics. Recent work, however, reveals that filaments created by two major regulators, the formins and the Arp2/3 complex, incorporate monomers delivered by nearby proteins. Specifically, actin enters Arp2/3-generated networks via binding sites on nucleation-promoting factors clustered on membrane surfaces. Here, we describe three functions of this surface-associated actin monomer pool: (1) regulating network density via product inhibition of the Arp2/3 complex, (2) accelerating filament elongation as a distributive polymerase, and (3) converting profilin-actin into a substrate for the Arp2/3 complex. These linked functions control the architecture of branched networks and explain how capping protein enhances their growth.

Indexed as

Actin cytoskeletonActin filamentArp2/3 complexBranched actin networkCapping proteinWASP family protein

Identifiers

PMID30470968
PMCPMC6297094
OpenAlexW2894924203

What OpenQuestion holds

Textmetadata
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.