Inhibition of “self” engulfment through deactivation of myosin-II at the phagocytic synapse between human cells

Tsai, Richard K.; Discher, Dennis E.

doi:10.1083/jcb.200708043

Cited by 486Phagocytosis and Immune RegulationCellular transport and secretionInvertebrate Immune Response Mechanisms

Inhibition of “self” engulfment through deactivation of myosin-II at the phagocytic synapse between human cells

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Tsai, Richard K., Discher, Dennis E.·2008·The Journal of Cell Biology

DOI 10.1083/jcb.200708043PMC PMC2265407

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Abstract

Phagocytosis of foreign cells or particles by macrophages is a rapid process that is inefficient when faced with “self” cells that display CD47—although signaling mechanisms in self-recognition have remained largely unknown. With human macrophages, we show the phagocytic synapse at cell contacts involves a basal level of actin-driven phagocytosis that, in the absence of species-specific CD47 signaling, is made more efficient by phospho-activated myosin. We use “foreign” sheep red blood cells (RBCs) together with CD47-blocked, antibody-opsonized human RBCs in order to visualize synaptic accumulation of phosphotyrosine, paxillin, F-actin, and the major motor isoform, nonmuscle myosin-IIA. When CD47 is functional, the macrophage counter-receptor and phosphatase-activator SIRPα localizes to the synapse, suppressing accumulation of phosphotyrosine and myosin without affecting F-actin. On both RBCs and microbeads, human CD47 potently inhibits phagocytosis as does direct inhibition of myosin. CD47–SIRPα interaction initiates a dephosphorylation cascade directed in part at phosphotyrosine in myosin. A point mutation turns off this motor's contribution to phagocytosis, suggesting that self-recognition inhibits contractile engulfment.

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CD47 binding to SIRPa on phagocytes inhibits cytoskeletal rearrangement and prevents engulfment.
“By binding to its cognate receptor SIRPa (also known as SHPS1) on the phagocyte, CD47 inhibits cytoskeletal rearrangement to prevent cell engulfment208.”
From Inflammation and its resolution in atherosclerosis: mediators and therapeutic opportunities (2019) · cites this paper as [208]

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Authors: Tsai, R. K., & Discher, D. E.
Affiliations: 1Biophysical Engineering Laboratory,
University of Pennsylvania (US)
ORCID: Discher, Dennis E.
Venue: The Journal of Cell Biology
Publisher: Rockefeller University Press
Published: 2008-03-10
Volume: 180
Issue: 5
Pages: 989-1003
ISSN: 0021-9525 (ISSN-L)
1540-8140
DOI: 10.1083/jcb.200708043
PMC: PMC2265407
OpenAlex: W2141638428
Cited by: 486
References: 71
Citations by year: 2026: 29 · 2025: 31 · 2024: 41 · 2023: 46 · 2022: 48 · 2021: 39 · 2020: 44 · 2019: 25 · 2018: 17 · 2017: 30 · 2016: 19 · 2015: 21 · 2014: 14 · 2013: 23 · 2012: 20
FWCI: 5.43
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: The Journal of Cell Biology (publishedVersion)
PubMed Central (publishedVersion, cc-by-nc-sa)
PubMed (publishedVersion)
ScholarlyCommons (University of Pennsylvania) (submittedVersion)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Phagocytosis and Immune Regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Life Sciences › Immunology and Microbiology › Immunology › Invertebrate Immune Response Mechanisms
Keywords: phagocytosis, self-recognition, CD47, SIRPα, myosin IIA, non-muscle myosin, macrophages, phosphotyrosine, paxillin, actin, sheep red blood cells, opsonization, dephosphorylation
MeSH terms: Actins, Animals, Antigens, Differentiation, Cell Communication, Chlorocebus aethiops, Cricetulus, Cricetinae, Humans, Intercellular Junctions, Macrophages, Phagocytosis, Phosphorylation, Receptors, Immunologic, Sheep, Synapses, CHO Cells, Point Mutation, Phosphotyrosine, COS Cells, Nonmuscle Myosin Type IIA, Paxillin, CD47 Antigen

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Inhibition of “self” engulfment through deactivation of myosin-II at the phagocytic synapse between human cells

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