ArticleThe Journal of cell biology2006
Two distinct cytoplasmic regions of the beta2 integrin chain regulate RhoA function during phagocytosis.
Article in The Journal of cell biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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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.
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.
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Who cites it
28 citing papers in PubMed, 68 citations in OpenAlex.
- A crosstalk between adhesion and phagocytosis integrates macrophage functions into their microenvironment.iScience · 2025Article
- Phagocytosis.Methods in molecular biology (Clifton, N.J.) · 2024Review
- Pathogenic single nucleotide polymorphisms in RhoA gene: Insights into structural and functional impacts on RhoA-PLD1 interaction through molecular dynamics simulation.Current research in structural biology · 2024Article
- Complement Activation in the Treatment of B-Cell Malignancies.Antibodies (Basel, Switzerland) · 2020Review
- RHOA-mediated mechanical force generation through Dectin-1.Journal of cell science · 2020Article
- Phagocytic Integrins: Activation and Signaling.Frontiers in immunology · 2020Review
- Identification of DNA methylation patterns predisposing for an efficient response to BCG vaccination in healthy BCG-naïve subjects.Epigenetics · 2019Article
- A Small GTPase, RhoA, Inhibits Bacterial Infection Through Integrin Mediated Phagocytosis in Invertebrates.Frontiers in immunology · 2018Article
- Phagocytosis: A Fundamental Process in Immunity.BioMed research international · 2017Review
- Apoptotic cell recognition receptors and scavenger receptors.Immunological reviews · 2016Review
- Phosphoinositide 3-kinase enables phagocytosis of large particles by terminating actin assembly through Rac/Cdc42 GTPase-activating proteins.Nature communications · 2015Article
- Regulation of phagocytosis by Rho GTPases.Small GTPases · 2015Review
- Leukocyte arrest: Biomechanics and molecular mechanisms of β2 integrin activation.Biorheology · 2015Review
- Porphyromonas gingivalis manipulates complement and TLR signaling to uncouple bacterial clearance from inflammation and promote dysbiosis.Cell host & microbe · 2014Article
- Resequencing the susceptibility gene, ITGAM, identifies two functionally deleterious rare variants in systemic lupus erythematosus cases.Arthritis research & therapy · 2014Article
- Regulator of G-Protein Signalling-14 (RGS14) Regulates the Activation of αMβ2 Integrin during Phagocytosis.PloS one · 2013Article
- Galectin-3 modulates phagocytosis-induced stellate cell activation and liver fibrosis in vivo.American journal of physiology. Gastrointestinal and liver physiology · 2012Article
- Ras-related GTPases Rap1 and RhoA collectively induce the phagocytosis of serum-opsonized zymosan particles in macrophages.The Journal of biological chemistry · 2012Article
- Interaction of two phagocytic host defense systems: Fcγ receptors and complement receptor 3.The Journal of biological chemistry · 2011Article
- Intracellular invasion by Orientia tsutsugamushi is mediated by integrin signaling and actin cytoskeleton rearrangements.Infection and immunity · 2010Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
AlphaMbeta2 integrins mediate phagocytosis of opsonized particles in a process controlled by RhoA, Rho kinase, myosin II, Arp2/3, and actin polymerization. AlphaMbeta2, Rho, Arp2/3, and F-actin accumulate underneath bound particles; however, the mechanism regulating Rho function during alphaMbeta2-mediated phagocytosis is poorly understood. We report that the binding of C3bi-opsonized sheep red blood cells (RBCs) to alphaMbeta2 increases Rho-GTP, but not Rac-GTP, levels. Deletion of the cytoplasmic domain of beta2, but not of alphaM, abolished Rho recruitment and activation, as well as phagocytic uptake. Interestingly, a 16-amino acid (aa) region in the membrane-proximal half of the beta2 cytoplasmic domain was necessary for activating Rho. Three COOH-terminal residues (aa 758-760) were essential for beta2-induced accumulation of Rho at complement receptor 3 (CR3) phagosomes. Activation of Rho was necessary, but not sufficient, for its stable recruitment underneath bound particles or for uptake. However, recruitment of active Rho was sufficient for phagocytosis. Our data shed light on the mechanism of outside-in signaling, from ligated integrins to the activation of Rho GTPase signaling.
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Registered trials
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.