F c RECEPTOR BIOLOGY
Abstract
This review deals with membrane Fc receptors (FcR) of the immunoglobulin superfamily. It is focused on the mechanisms by which FcR trigger and regulate biological responses of cells on which they are expressed. FcR deliver signals when they are aggregated at the cell surface. The aggregation of FcR having immunoreceptor tyrosine-based activation motifs (ITAMs) activates sequentially src family tyrosine kinases and syk family tyrosine kinases that connect transduced signals to common activation pathways shared with other receptors. FcR with ITAMs elicit cell activation, endocytosis, and phagocytosis. The nature of responses depends primarily on the cell type. The aggregation of FcR without ITAM does not trigger cell activation. Most of these FcR internalize their ligands, which can be endocytosed, phagocytosed, or transcytosed. The fate of internalized receptor-ligand complexes depends on defined sequences in the intracytoplasmic domain of the receptors. The coaggregation of different FcR results in positive or negative cooperation. Some FcR without ITAM use FcR with ITAM as signal transduction subunits. The coaggregation of antigen receptors or of FcR having ITAMs with FcR having immunoreceptor tyrosine-based inhibition motifs (ITIMs) negatively regulates cell activation. FcR therefore appear as the subunits of multichain receptors whose constitution is not predetermined and which deliver adaptative messages as a function of the environment.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Fcγ receptors bind specifically to IgG on antibody-coated particles.
“These include the Fcγ receptors (FcγRs), that bind specifically to the IgG found on antibody-coated particles (Daeron 1997).”
From Localized Biphasic Changes in Phosphatidylinositol-4,5-Bisphosphate at Sites of Phagocytosis (2000) · cites this paper as Daeron 1997
Cites
Raghavan, M., Bonagura, V. R., Morrison, S. L., & Bjorkman, P. J. (1995) · Biochemistry · doi:10.1021/bi00045a005 · Cited by 317 · see citing works
Greenberg, S., Chang, P., & Silverstein, S. C. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41945-4 · Cited by 237 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Bruhns, P., Iannascoli, B., England, P., Mancardi, D. A., Fernandez, N., Jorieux, S., & Daëron, M. (2009) · Blood · doi:10.1182/blood-2008-09-179754 · Cited by 1,479 · see citing works
Self-citationThe SYK tyrosine kinase: A crucial player in diverse biological functions
Mócsai, A., Ruland, J., & Tybulewicz, V. L. J. (2010) · Nature Reviews Immunology · doi:10.1038/nri2765 · Cited by 1,368 · see citing works
THE HIGH-AFFINITY I <scp>g</scp> E RECEPTOR (FcεRI): From Physiology to Pathology
Kinet, J.-P. (1999) · Annual Review of Immunology · doi:10.1146/annurev.immunol.17.1.931 · Cited by 968 · see citing works
Antimicrobial mechanisms of phagocytes and bacterial evasion strategies
Flannagan, R. S., Cosío, G., & Grinstein, S. (2009) · Nature Reviews Microbiology · doi:10.1038/nrmicro2128 · Cited by 947 · see citing works
Localized Biphasic Changes in Phosphatidylinositol-4,5-Bisphosphate at Sites of Phagocytosis
Botelho, R. J., Teruel, M., Dierckman, R., Anderson, R., Wells, A., York, J. D., Meyer, T., & Grinstein, S. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.7.1353 · Cited by 539 · see citing works
“These include the Fc g receptors (Fc g Rs), 1 that bind specifically to the IgG found on antibody-coated particles (Daeron, 1997).”
BackgroundPhospholipase Cγ2 Is Essential in the Functions of B Cell and Several Fc Receptors
Wang, D., Feng, J., Wen, R., Marine, J.-C., Sangster, M. Y., Parganas, E., Hoffmeyer, A., Jackson, C. W., Cleveland, J. L., Murray, P. J., et al. (2000) · Immunity · doi:10.1016/s1074-7613(00)00005-4 · Cited by 475 · see citing works
Phagocytosis of Retinal Rod and Cone Photoreceptors
Kevany, B. M., & Palczewski, K. (2010) · Physiology · doi:10.1152/physiol.00038.2009 · Cited by 426 · see citing works
“Recognition of substrates by the macrophage results in recruitment of Fc R to the site of contact, resulting in the initiation of a phosphorylation cascade involving a number of kinases (16, 30).”
BackgroundImmunogenicity of protein therapeutics: The key causes, consequences and challenges
Baker, M., Reynolds, H. M., Lumicisi, B., & Bryson, C. J. (2010) · Self/Nonself · doi:10.4161/self.1.4.13904 · Cited by 372 · see citing works
The cytoskeleton in phagocytosis and macropinocytosis
Mylvaganam, S., Freeman, S. A., & Grinstein, S. (2021) · Current Biology · doi:10.1016/j.cub.2021.01.036 · Cited by 263 · see citing works
Wilkinson, M. B., Xiao, G., Kumar, A., LaPlant, Q., Renthal, W., Sikder, D., Kodadek, T. J., & Nestler, E. J. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.0932-09.2009 · Cited by 262 · see citing works
Harms, A. S., Thome, A. D., Yan, Z., Schonhoff, A. M., Williams, G. P., Li, X., Liu, Y., Qin, H., Benveniste, E. N., & Standaert, D. G. (2018) · Experimental Neurology · doi:10.1016/j.expneurol.2017.11.010 · Cited by 236 · see citing works
Signal Transduction by the High-Affinity Immunoglobulin E Receptor FcεRI: Coupling Form to Function
Nadler, M. J. S., Matthews, S. A., Turner, H., & Kinet, J.-P. (2001) · Advances in Immunology · doi:10.1016/s0065-2776(01)76022-1 · Cited by 203 · see citing works
A chimeric human-cat fusion protein blocks cat-induced allergy
Zhu, D., Kepley, C. L., Zhang, K., Terada, T., Yamada, T., & Saxon, A. (2005) · Nature Medicine · doi:10.1038/nm1219 · Cited by 188 · see citing works
Tse, S. M. L., Furuya, W., Gold, E., Schreiber, A. D., Sandvig, K., Inman, R. D., & Grinstein, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m207966200 · Cited by 124 · see citing works
The Development of Serum Amyloid P as a Possible Therapeutic
Pilling, D., & Gomer, R. H. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02328 · Cited by 92 · see citing works
“Once aggregated IgG cross-links multiple FcγRs (this prevents monomeric IgGs from activating FcγRs), a signaling cascade is activated through tyrosine kinases to initiate an immune response (151).”
BackgroundHarnessing and Enhancing Macrophage Phagocytosis for Cancer Therapy
Chen, S., Lai, S. W. T., Brown, C. E., & Feng, M. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.635173 · Cited by 91 · see citing works
“Within the human FcgR family, all but FcgRIIB are immunoreceptor tyrosine-based activation motif (ITAM) bearing activating FcRs that activate upon binding to IgGs via multimerization of intracellular ITAM domains (24, 26).”
BackgroundSHP-1 regulates Fcγ receptor–mediated phagocytosis and the activation of RAC
Kant, A. M., De, P., Peng, X., Yi, T., Rawlings, D. J., Kim, J. S., & Durden, D. L. (2002) · Blood · doi:10.1182/blood.v100.5.1852.h81702001852_1852_1859 · Cited by 81 · see citing works
Channel catfish NK-like cells are armed with IgM via a putative FcμR
Shen, L., Stuge, T. B., Evenhuis, J. P., Bengtén, E., Wilson, M., Chinchar, V. G., Clem, L. W., & Miller, N. W. (2003) · Developmental & Comparative Immunology · doi:10.1016/s0145-305x(03)00042-9 · Cited by 82 · see citing works
FcγRIII Expression on Cultured Human Keratinocytes and Upregulation by Interferon-γ
Cauza, K., Grassauer, A., Hinterhuber, G., Wolff, K., Foedinger, D., Horvat, R., & Rappersberger, K. (2002) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2002.19527.x · Cited by 21 · see citing works
- Authors
- Daëron, M.
- Affiliations
- Inserm (FR)
- Corresponding author
- Daëron, Marc
- ORCID
- Daëron, Marc
- Venue
- Annual Review of Immunology
- Publisher
- Annual Reviews
- Published
- 1997-04
- Volume
- 15
- Issue
- 1
- Pages
- 203-234
- ISSN
- 0732-0582 (ISSN-L)
- 1545-3278
- OpenAlex
- W2154901790
- Cited by
- 1,227
- References
- 2
- Citations by year
- 2026: 14 · 2025: 11 · 2024: 18 · 2023: 16 · 2022: 18 · 2021: 21 · 2020: 25 · 2019: 29 · 2018: 20 · 2017: 24 · 2016: 24 · 2015: 37 · 2014: 31 · 2013: 32 · 2012: 52
- FWCI
- 15.56
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Immunology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- Fc receptors, immunoglobulin superfamily, signal transduction, receptor aggregation, ITAM, ITIM, Src family kinases, receptor internalization, phagocytosis, endocytosis, transcytosis
- MeSH terms
- Animals, Humans, Models, Biological, Protein-Tyrosine Kinases, Receptor Aggregation, Receptors, Fc, Tyrosine, Molecular Structure, Signal Transduction
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
