Evidence map›Paper›PMID 34708690›Full record

ArticleeLife2021

Phagocytic 'teeth' and myosin-II 'jaw' power target constriction during phagocytosis.

Daan Vorselen, Sarah R Barger, Yifan Wang, Wei Cai, Julie A Theriot, Nils C Gauthier, Mira Krendel

Open access · goldAbstract read
In one paragraph

Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed, 1 pooled it
5.6field-weighted citation impact, top 3% 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

52 citing papers in PubMed, 1 synthesis or guideline pooled it, 86 citations in OpenAlex.

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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 4 institutions in 2 countries.

Daan Vorselen *Department of Biology and Howard Hughes Medical Institute, University of Washington, Seattle, United States.ORCID 0000-0002-7800-4023
Sarah R Barger *Department of Cell and Developmental Biology, State University of New York Upstate Medical University, Syracuse, United States.ORCID 0000-0002-6941-7256
Yifan WangDepartment of Mechanical Engineering, Stanford University, Stanford, United States.
Wei CaiDepartment of Mechanical Engineering, Stanford University, Stanford, United States.
Julie A TheriotDepartment of Biology and Howard Hughes Medical Institute, University of Washington, Seattle, United States.ORCID 0000-0002-2334-2535
Nils C GauthierIFOM, FIRC Institute of Molecular Oncology, Milan, Italy.
Mira KrendelDepartment of Cell and Developmental Biology, State University of New York Upstate Medical University, Syracuse, United States.ORCID 0000-0002-7008-9069
Howard Hughes Medical Institute · USStanford University · USSUNY Upstate Medical University · USIFOM · IT

Funding

Role of myosin 1e in podocyte biology and renal filtrationR01DK083345 · NIDDK · UPSTATE MEDICAL UNIVERSITY · PI Mira Krendel · 2011 to 2026
$6.8M
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 InstituteNIDDK NIH HHS R01 DK083345NIGMS NIH HHS R01 GM138652
6 · The paper itself

Abstract

Phagocytosis requires rapid actin reorganization and spatially controlled force generation to ingest targets ranging from pathogens to apoptotic cells. How actomyosin activity directs membrane extensions to engulf such diverse targets remains unclear. Here, we combine lattice light-sheet microscopy (LLSM) with microparticle traction force microscopy (MP-TFM) to quantify actin dynamics and subcellular forces during macrophage phagocytosis. We show that spatially localized forces leading to target constriction are prominent during phagocytosis of antibody-opsonized targets. This constriction is largely driven by Arp2/3-mediated assembly of discrete actin protrusions containing myosin 1e and 1f ('teeth') that appear to be interconnected in a ring-like organization. Contractile myosin-II activity contributes to late-stage phagocytic force generation and progression, supporting a specific role in phagocytic cup closure. Observations of partial target eating attempts and sudden target release via a popping mechanism suggest that constriction may be critical for resolving complex in vivo target encounters. Overall, our findings present a phagocytic cup shaping mechanism that is distinct from cytoskeletal remodeling in 2D cell motility and may contribute to mechanosensing and phagocytic plasticity.

Indexed as

ActinsAnimalsBone Marrow CellsCytoskeletonHL-60 CellsHumansMacrophagesMiceMice, Inbred C57BLMicroscopyMolecular ImagingMyosin Type IIPhagocytosisRAW 264.7 CellsStem CellsActinsMyosin Type IIactincell biologycytoskeletonmousemyosinphagocytosisphysics of living systems

Identifiers

PMID34708690
PMCPMC8585483
OpenAlexW3210478861

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.