Evidence map›Paper›PMID 36129777›Full record

ArticleMolecular biology of the cell2022

F-actin organization and target constriction during primary macrophage phagocytosis is balanced by competing activity of myosin-I and myosin-II.

Sarah R Barger, Daan Vorselen, Nils C Gauthier, Julie A Theriot, Mira Krendel

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Macrophage Actin Cytoskeleton in Chronic Rejection.Results and problems in cell differentiation · 2026
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Dynamics of phagocytosis mediated by phosphatidylserine.Biochemical Society transactions · 2022
    Review
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

5 authors at 3 institutions in 3 countries.

Sarah R BargerDepartment of Cell and Developmental Biology, State University of New York Upstate Medical University, Syracuse, NY 13210.
Daan VorselenDepartment of Biology and Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195.
Nils C GauthierIFOM, FIRC Institute of Molecular Oncology, Milan, Italy.
Julie A TheriotDepartment of Biology and Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195.
Mira KrendelDepartment of Cell and Developmental Biology, State University of New York Upstate Medical University, Syracuse, NY 13210.
Howard Hughes Medical Institute · USSUNY Upstate Medical University · USIFOM · IT

Funding

Class I myosins regulate protrusive forces at the actin-membrane interfaceR01GM138652 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI KRENDEL, MIRA, SIROTKIN, VLADIMIR A · 2021 to 2024
$2.4M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM138652
6 · The paper itself

Abstract

Phagocytosis requires rapid remodeling of the actin cytoskeleton for extension of membrane protrusions and force generation to ultimately drive the engulfment of targets. The detailed mechanisms of phagocytosis have almost exclusively been studied in immortalized cell lines. Here, we make use of high-resolution imaging and novel biophysical approaches to determine the structural and mechanical features of phagocytosis by primary bone marrow-derived macrophages. We find that the signature behavior of these primary cells is distinct from macrophage-like cell lines; specifically, it is gentle, with only weak target constriction and modest polarization of the F-actin distribution inside the phagocytic cup. We show that long-tailed myosins 1e/f are critical for this organization. Deficiency of myo1e/f causes dramatic shifts in F-actin localization, reducing F-actin at the phagocytic cup base and enhancing F-actin-mediated constriction at the cup rim. Surprisingly, these changes can be almost fully reverted upon inhibition of another myosin motor protein, myosin-II. Hence, we show that the biomechanics and large-scale organization of phagocytic cups is tightly regulated through competing contributions from myosin-Ie/f and myosin-II.

Indexed as

ActinsPhagocytosisActin CytoskeletonConstrictionCytoskeletal ProteinsMacrophagesMyosinsMyosin Type IIActinsCytoskeletal ProteinsMyosinsMyosin Type II

Identifiers

PMID36129777
PMCPMC9727803
OpenAlexW4296552752

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.