Journal articles: 'Fc receptor-like'

1

Davis, Randall S. "Fc Receptor-Like Molecules." Annual Review of Immunology 25, no. 1 (April 2007): 525–60. http://dx.doi.org/10.1146/annurev.immunol.25.022106.141541.

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Maltais, Lois J., Ruth C. Lovering, Alexander V. Taranin, Marco Colonna, Jeffrey V. Ravetch, Riccardo Dalla-Favera, Peter D. Burrows, Max D. Cooper, and Randall S. Davis. "New nomenclature for Fc receptor–like molecules." Nature Immunology 7, no. 5 (May 2006): 431–32. http://dx.doi.org/10.1038/ni0506-431.

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Lennartz, Michelle, and James Drake. "Molecular mechanisms of macrophage Toll-like receptor–Fc receptor synergy." F1000Research 7 (January 8, 2018): 21. http://dx.doi.org/10.12688/f1000research.12679.1.

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Macrophages (MØs) are a key cell type of both the innate and the adaptive immune response and can tailor their response to prevailing conditions. To sense the host’s status, MØs employ two classes of receptors: Toll-like receptors (TLRs), which are sensors for pathogen-derived material, and Fcγ receptors (FcγRs) that are detectors of the adaptive immune response. How MØs integrate the input from these various sensors is not understood and is the focus of active study. Here, we review the recent literature on the molecular mechanisms of TLR and FcgR crosstalk and synergy, and discuss the implications of these findings. This overview suggests a multilayered mechanism of receptor synergy that allows the MØ to fine-tune its response to prevailing conditions and provides ideas for future investigation.

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Abdollahi-Roodsaz, S., M. I. Koenders, P. L. van Lent, F. A. van de Loo, and W. B. van den Berg. "Toll-like receptor 2 negatively regulates Fc receptor response in macrophages and inhibits Fc R-mediated arthritis." Annals of the Rheumatic Diseases 70, Suppl 2 (February 22, 2011): A36. http://dx.doi.org/10.1136/ard.2010.148973.2.

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Silberstein, Erica, Gabriela Dveksler, and Gerardo G. Kaplan. "Neutralization of Hepatitis A Virus (HAV) by an Immunoadhesin Containing the Cysteine-Rich Region of HAV Cellular Receptor-1." Journal of Virology 75, no. 2 (January 15, 2001): 717–25. http://dx.doi.org/10.1128/jvi.75.2.717-725.2001.

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ABSTRACT Hepatitis A virus (HAV) infects African green monkey kidney (AGMK) cells via the HAV cellular receptor-1 (havcr-1), a mucin-like type 1 integral-membrane glycoprotein of unknown natural function. The ectodomain of havcr-1 contains an N-terminal immunoglobulin-like cysteine-rich region (D1), which binds protective monoclonal antibody (MAb) 190/4, followed by an O-glycosylated mucin-like threonine-serine-proline-rich region that extends D1 well above the cell surface. To study the interaction of HAV with havcr-1, we constructed immunoadhesins fusing the hinge and Fc portion of human IgG1 to D1 (D1-Fc) or the ectodomain of the poliovirus receptor (PVR-Fc) and expressed them in CHO cells. These immunoadhesins were secreted to the cell culture medium and purified through protein A-agarose columns. In a solid-phase assay, HAV bound to D1-Fc in a concentration-dependent manner whereas background levels of HAV bound to PVR-Fc. Binding of HAV to D1-Fc was blocked by treatment with MAb 190/4 but not with control MAb M2, which binds to a tag epitope introduced between the D1 and Fc portions of the immunoadhesin. D1-Fc neutralized approximately 1 log unit of the HAV infectivity in AGMK cells, whereas PVR-Fc had no effect in the HAV titers. A similarly poor reduction in HAV titers was observed after treating the same stock of HAV with murine neutralizing MAbs K2-4F2, K3-4C8, and VHA 813. Neutralization of poliovirus by PVR-Fc but not by D1-Fc indicated that the virus-receptor interactions were specific. These results show that D1 is sufficient for binding and neutralization of HAV and provide further evidence that havcr-1 is a functional cellular receptor for HAV.

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Franco, Andrea, Bazarragchaa Damdinsuren, Tomoko Ise, Jessica Dement-Brown, Huifang Li, Satoshi Nagata, and Mate Tolnay. "Human Fc Receptor–Like 5 Binds Intact IgG via Mechanisms Distinct from Those of Fc Receptors." Journal of Immunology 190, no. 11 (April 24, 2013): 5739–46. http://dx.doi.org/10.4049/jimmunol.1202860.

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Shang, Limin, Bruno Daubeuf, Martha Triantafilou, Robin Olden, Fabien Dépis, Anne-Catherine Raby, Suzanne Herren, et al. "Selective Antibody Intervention of Toll-like Receptor 4 Activation through Fc γ Receptor Tethering." Journal of Biological Chemistry 289, no. 22 (April 15, 2014): 15309–18. http://dx.doi.org/10.1074/jbc.m113.537936.

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Silberstein, Erica, Li Xing, Willem van de Beek, Jinhua Lu, Holland Cheng, and Gerardo G. Kaplan. "Alteration of Hepatitis A Virus (HAV) Particles by a Soluble Form of HAV Cellular Receptor 1 Containing the Immunoglobulin- and Mucin-Like Regions." Journal of Virology 77, no. 16 (August 15, 2003): 8765–74. http://dx.doi.org/10.1128/jvi.77.16.8765-8774.2003.

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ABSTRACT Hepatitis A virus (HAV) infects African green monkey kidney cells via HAV cellular receptor 1 (havcr-1). The ectodomain of havcr-1 contains an N-terminal cysteine-rich immunoglobulin-like region (D1), followed by a mucin-like region that extends D1 well above the cell surface. D1 is required for binding of HAV, and a soluble construct containing D1 fused to the hinge and Fc portions of human immunoglobulin G1 (IgG1), D1-Fc, bound and neutralized HAV inefficiently. However, D1-Fc did not alter the virions. To determine whether additional regions of havcr-1 are required to trigger uncoating of HAV, we constructed D1muc-Fc containing D1 and two-thirds of the mucin-like region fused to the Fc and hinge portions of human IgG1. D1muc-Fc neutralized 10 times more HAV than did D1-Fc. Sedimentation analysis in sucrose gradients showed that treatment of HAV with 20 to 200 nM D1muc-Fc disrupted the majority of the virions, whereas treatment with 2 nM D1muc-Fc had no effect on the sedimentation of the particles. Treatment of HAV with 100 nM D1muc-Fc resulted in low-level accumulation of 100- to 125S particles. Negative-stain electron microscopy analysis revealed that the 100- to 125S particles had the characteristics of disrupted virions, such as internal staining and diffuse edges. Quantitative PCR analysis showed that the 100- to 125S particles contained viral RNA. These results indicate that D1 and the mucin-like region of havcr-1 are required to induce conformational changes leading to HAV uncoating.

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Kacskovics, Imre, Zhen Wu, Neil E. Simister, László V. Frenyó, and Lennart Hammarström. "Cloning and Characterization of the Bovine MHC Class I-Like Fc Receptor." Journal of Immunology 164, no. 4 (February 15, 2000): 1889–97. http://dx.doi.org/10.4049/jimmunol.164.4.1889.

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Li, Huifang, Jessica Dement-Brown, Pei-Jyun Liao, Ilya Mazo, Frederick Mills, Zachary Kraus, Sean Fitzsimmons, and Mate Tolnay. "Fc receptor-like 4 and 5 define human atypical memory B cells." International Immunology 32, no. 12 (August 17, 2020): 755–70. http://dx.doi.org/10.1093/intimm/dxaa053.

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Abstract Atypical memory B cells accumulate in chronic infections and autoimmune conditions, and commonly express FCRL4 and FCRL5, respective IgA and IgG receptors. We characterized memory cells from tonsils on the basis of both FCRL4 and FCRL5 expression, defining three subsets with distinct surface proteins and gene expression. Atypical FCRL4+FCRL5+ memory cells had the most discrete surface protein expression and were enriched in cell adhesion pathways, consistent with functioning as tissue-resident cells. Atypical FCRL4−FCRL5+ memory cells expressed transcription factors and immunoglobulin genes that suggest poised differentiation into plasma cells. Accordingly, the FCRL4−FCRL5+ memory subset was enriched in pathways responding to endoplasmic reticulum stress and IFN-γ. We reconstructed ongoing B-cell responses as lineage trees, providing crucial in vivo developmental context. Each memory subset typically maintained its lineage, denoting mechanisms enforcing their phenotypes. Classical FCRL4−FCRL5− memory cells were infrequently detected in lineage trees, suggesting the majority were in a quiescent state. FCRL4−FCRL5+ cells were the most represented memory subset in lineage trees, indicating robust participation in ongoing responses. Together, these differences suggest FCRL4 and FCRL5 are unlikely to be passive markers but rather active drivers of human memory B-cell development and function.

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Akilesh, Shreeram, Stefka Petkova, Thomas J. Sproule, Daniel J. Shaffer, Gregory J. Christianson, and Derry Roopenian. "The MHC class I–like Fc receptor promotes humorally mediated autoimmune disease." Journal of Clinical Investigation 113, no. 9 (May 1, 2004): 1328–33. http://dx.doi.org/10.1172/jci18838.

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12

Akilesh, S. "The MHC class I-like Fc receptor promotes humorally mediated autoimmune disease." Journal of Clinical Investigation 113, no. 9 (May 1, 2004): 1328–33. http://dx.doi.org/10.1172/jci200418838.

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13

Zhong, Zhong, Dianchun Shi, Mengjiao Xiao, Dongying Fu, Shaozhen Feng, Qingyu Kong, Jianbo Li, and Zhijian Li. "Expression profile of Fc receptor-like molecules in patients with IgA nephropathy." Human Immunology 82, no. 3 (March 2021): 186–92. http://dx.doi.org/10.1016/j.humimm.2021.01.011.

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14

Salmon, J. E., S. Kapur, and R. P. Kimberly. "Opsonin-independent ligation of Fc gamma receptors. The 3G8-bearing receptors on neutrophils mediate the phagocytosis of concanavalin A-treated erythrocytes and nonopsonized Escherichia coli." Journal of Experimental Medicine 166, no. 6 (December 1, 1987): 1798–813. http://dx.doi.org/10.1084/jem.166.6.1798.

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We report that phagocytosis by human neutrophils of Con A-treated erythrocytes (E-Con A) and nonopsonized Escherichia coli with mannose-binding adhesions is mediated by the Fc gamma receptor bearing the 3G8 epitope. Modulation of Fc receptors by pretreating with aggregated-IgG or with 3G8 anti-Fc gamma receptor mAb markedly inhibited internalization of E-Con A and E. coli without altering their cell surface attachment. Phagocytosis of these probes was specifically blocked by alpha-methylmannoside and D-mannose and not by other monosaccharides. Thus, recognition of E-Con A and E. coli by the Fc receptor is dependent upon the mannose-specific interaction with lectin or lectin-like adhesions. These data demonstrate that ligands other than the classical IgG opsonins can bind to classical immune receptors for IgG through lectin-carbohydrate interactions.

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Warmerdam, P. A., J. G. van de Winkel, E. J. Gosselin, and P. J. Capel. "Molecular basis for a polymorphism of human Fc gamma receptor II (CD32)." Journal of Experimental Medicine 172, no. 1 (July 1, 1990): 19–25. http://dx.doi.org/10.1084/jem.172.1.19.

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The IgG Fc receptor II on human monocytes is polymorphic in its ability to bind mIgG1, and its isoelectric focusing pattern. To study the molecular basis of this polymorphism, a cDNA library from cell line K562, expressing two different allelic forms (high responder [HR] and low responder [LR]) of Fc gamma RII, was used for cDNA cloning. We report the isolation and identification of different Fc gamma RII cDNA clones, comprising the LR form of Fc gamma RII, as was evident from studies using a new HR-specific anti-Fc gamma RII mAb 41H16, and from rosetting experiments. Sequence analysis revealed that HR and LR forms differ by two amino acids, both located in the external domain. In the cloned LR form, a glutamine is substituted by a tryptophan residue at aa position 27, located in the first Ig-like domain, and an arginine residue by a histidine residue at aa position 131 in the second Ig-like domain. Furthermore, an Fc gamma RII cDNA clone was isolated with a deletion of 123 bp, overlapping the predicted transmembrane segment. Data showing the presence of an alternatively spliced mRNA detected by using polymerase chain reaction (PCR) might suggest the existence of a soluble form of the human Fc gamma RII, in addition to the membrane-bound forms.

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Roberts, D. M., M. Guenthert, and R. Rodewald. "Isolation and characterization of the Fc receptor from the fetal yolk sac of the rat." Journal of Cell Biology 111, no. 5 (November 1, 1990): 1867–76. http://dx.doi.org/10.1083/jcb.111.5.1867.

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The yolk sac of the fetal rat and the proximal small intestine of the neonatal rat selectively transport maternal IgG. IgG-Fc receptors are thought to mediate transport across the epithelium of both tissues. We used a mouse mAb (MC-39) against the 45-54-kD component of the Fc receptor of the neonatal intestine to find an antigenically related protein that might function as an Fc receptor in fetal yolk sac. In immunoblots of yolk sac, MC-39 recognized a protein band with apparent molecular mass of 54-58 kD. MC-39 bound to the endoderm of yolk sac in immunofluorescence studies. In immunogold-labeling experiments MC-39 was associated mainly with small vesicles in the apical cytoplasm and in the region near the basolateral membrane of endodermal cells. The MC-39 cross-reactive protein and beta 2-microglobulin, a component of the intestinal Fc receptor, were copurified from detergent-solubilized yolk sac by an affinity purification that selected for proteins which, like the intestinal receptor, bound to IgG at pH 6.0 and eluted at pH 8.0. In summary, the data suggest that we have isolated the Fc receptor of the yolk sac and that this receptor is structurally and functionally related to the Fc receptor of the neonatal intestine. An unexpected finding is that, unlike the intestinal receptor which binds maternal IgG on the apical cell surface, the yolk sac receptor appears to bind IgG only within apical compartments which we suggest represent the endosomal complex.

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Seizer, Peter, Oliver Borst, Harald Langer, Andreas Bültmann, Götz Münch, Yared Herouy, Konstantinos Stellos, et al. "EMMPRIN (CD147) is a novel receptor for platelet GPVI and mediates platelet rolling via GPVI-EMMPRIN interaction." Thrombosis and Haemostasis 101, no. 04 (2009): 682–86. http://dx.doi.org/10.1160/th08-06-0368.

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SummaryThe Extracellular Matrix Metalloproteinase Inducer (EMMPRIN, CD147, basigin) is an immunoglobulin-like receptor expressed in various cell types. During cellular interactions homotypic EMMPRIN-EMMPRIN interactions are known to induce the synthesis of matrix metalloproteinases. Recently, we have identified EMMPRIN as a novel receptor on platelets. To our knowledge EMMPRIN has not been shown to serve as adhesion receptor, yet. Here we characterise platelet glycoprotein VI (GPVI) as a novel adhesion receptor for EMMPRIN. Human platelets were prestimulated with ADP and perfused over immobilised recombinant EMMPRIN-Fc or Fc-fragments under arterial shear conditions. ADP-stimulated platelets showed significantly enhanced rolling (but not enhanced firm adhesion) on immobilised EMMPRIN-Fc compared to Fc. Pretreatment of platelets with blocking mAbs anti-EMMPRIN or anti-GPVI leads to a significant reduction of rolling platelets on immobilised EMMPRIN-Fc, whereas pretreatment with blocking mAbs anti-p-selectin, anti-α4-integrin or anti-GPIIb/IIIa complex (20 μg/ml each) had no effect. Consistently, chinese hamster ovary (CHO) cells stably transfected with GPVI showed enhanced rolling (but not adhesion) on immobilised EMMPRIN-Fc in comparison to nontransfected CHO cells. Similarly, CHO cells stably transfected with EMMPRIN showed enhanced rolling on immobilised GPVIFc (or EMMPRIN-Fc) compared to non transfected CHO-cells. Finally, specific binding of EMMPRIN to GPVI was demonstrated by a modified ELISA and surface plasmon resonance technology with a dissociation constant of 88 nM. Platelet GPVI is a novel receptor for EMMPRIN and can mediate platelet rolling via GPVIEMMPRIN interaction.

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de Taeye, Steven W., Theo Rispens, and Gestur Vidarsson. "The Ligands for Human IgG and Their Effector Functions." Antibodies 8, no. 2 (April 25, 2019): 30. http://dx.doi.org/10.3390/antib8020030.

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Activation of the humoral immune system is initiated when antibodies recognize an antigen and trigger effector functions through the interaction with Fc engaging molecules. The most abundant immunoglobulin isotype in serum is Immunoglobulin G (IgG), which is involved in many humoral immune responses, strongly interacting with effector molecules. The IgG subclass, allotype, and glycosylation pattern, among other factors, determine the interaction strength of the IgG-Fc domain with these Fc engaging molecules, and thereby the potential strength of their effector potential. The molecules responsible for the effector phase include the classical IgG-Fc receptors (FcγR), the neonatal Fc-receptor (FcRn), the Tripartite motif-containing protein 21 (TRIM21), the first component of the classical complement cascade (C1), and possibly, the Fc-receptor-like receptors (FcRL4/5). Here we provide an overview of the interactions of IgG with effector molecules and discuss how natural variation on the antibody and effector molecule side shapes the biological activities of antibodies. The increasing knowledge on the Fc-mediated effector functions of antibodies drives the development of better therapeutic antibodies for cancer immunotherapy or treatment of autoimmune diseases.

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Li, Yaxin, Guopeng Wang, Ningning Li, Yuxin Wang, Qinyu Zhu, Huarui Chu, Wenjun Wu, et al. "Structural insights into immunoglobulin M." Science 367, no. 6481 (February 6, 2020): 1014–17. http://dx.doi.org/10.1126/science.aaz5425.

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Immunoglobulin M (IgM) plays a pivotal role in both humoral and mucosal immunity. Its assembly and transport depend on the joining chain (J-chain) and the polymeric immunoglobulin receptor (pIgR), but the underlying molecular mechanisms of these processes are unclear. We report a cryo–electron microscopy structure of the Fc region of human IgM in complex with the J-chain and pIgR ectodomain. The IgM-Fc pentamer is formed asymmetrically, resembling a hexagon with a missing triangle. The tailpieces of IgM-Fc pack into an amyloid-like structure to stabilize the pentamer. The J-chain caps the tailpiece assembly and bridges the interaction between IgM-Fc and the polymeric immunoglobulin receptor, which undergoes a large conformational change to engage the IgM-J complex. These results provide a structural basis for the function of IgM.

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Hayakawa, Kazuhide, Loc-Duyen D. Pham, Ji Hae Seo, Nobukazu Miyamoto, Takakuni Maki, Yasukazu Terasaki, Sava Sakadžić, et al. "CD200 restrains macrophage attack on oligodendrocyte precursors via toll-like receptor 4 downregulation." Journal of Cerebral Blood Flow & Metabolism 36, no. 4 (September 30, 2015): 781–93. http://dx.doi.org/10.1177/0271678x15606148.

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There are numerous barriers to white matter repair after central nervous system injury and the underlying mechanisms remain to be fully understood. In this study, we propose the hypothesis that inflammatory macrophages in damaged white matter attack oligodendrocyte precursor cells via toll-like receptor 4 signaling thus interfering with this endogenous progenitor recovery mechanism. Primary cell culture experiments demonstrate that peritoneal macrophages can attack and digest oligodendrocyte precursor cells via toll-like receptor 4 signaling, and this phagocytosis of oligodendrocyte precursor cells can be inhibited by using CD200-Fc to downregulate toll-like receptor 4. In an in vivo model of white matter ischemia induced by endothelin-1, treatment with CD200-Fc suppressed toll-like receptor 4 expression in peripherally circulating macrophages, thus restraining macrophage phagocytosis of oligodendrocyte precursor cells and leading to improved myelination. Taken together, these findings suggest that deleterious macrophage effects may occur after white matter ischemia, whereby macrophages attack oligodendrocyte precursor cells and interfere with endogenous recovery responses. Targeting this pathway with CD200 may offer a novel therapeutic approach to amplify endogenous oligodendrocyte precursor cell-mediated repair of white matter damage in mammalian brain.

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Alabi, Oyeleye, Jessica Dement-Brown, and Mate Tolnay. "Human Fc receptor-like 5 distinguishes IgG2 disulfide isoforms and deamidated charge variants." Molecular Immunology 92 (December 2017): 161–68. http://dx.doi.org/10.1016/j.molimm.2017.10.020.

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Onizuka, Makoto, Masako Toyosaki, Shinichiro Machida, Rikio Suzuki, Minoru Kojima, Koichi Miyamura, Yoshihisa Kodera, Hidetoshi Inoko, and Kiyoshi Ando. "Association of Fc Receptor-Like Protein Family with Chronic Graft-Versus-Host Disease." Blood 110, no. 11 (November 16, 2007): 2970. http://dx.doi.org/10.1182/blood.v110.11.2970.2970.

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Abstract Chronic graft versus host disease (cGVHD) is the most common cause of poor outcomes after hematopoietic stem cell transplantation (HSCT), while the pathophysiology of cGVHD remains poorly understood. We have revealed the association Fc receptor-like protein 3 (FCRL3) gene -169C/T single nucleotide polymorphism (SNP) and developing cGVHD. This gene is a member of Fc receptor-like protein gene family which contains 5 genes and well known as autoimmune disease associated gene. These 5 genes make cluster lesion on chromosome 1q21 to 23. In this current study, to investigate the relationship with another Fc receptor-like protein genes and cGVHD, we used 4 microsatellite polymorphisms belong to FCRL1, 2, 3 and 4 as a linkage analysis genetic marker. And we also investigated FCRL3 -169C/T SNP and another 3 SNPs to explore haplotype and the incidence of cGVHD. We analyzed 123 case of Japanese HLA-matched sibling recipients and their donor who underwent HSCT in the Japanese Red-Cross Nagoya First hospital. Before day 100, 11 patients died from severe acute GVHD, infection, thrombotic microangiopathy or disease relapse. Therefore, we analyzed 112 recipients and 108 donors for the relationship between gene polymorphisms and chronic GVHD. We analyzed microsatellite polymorphisms and SNPs by using TaqMan® assay. Chronic GVHD occurred in 54 out of 112 (48.2%) patients in this cohort. The nearest microsatellite marker from FCRL3 gene had significant different allele frequency between cGVHD and non-GVHD recipient (p=0.0034). There were no association with another microsatellites allele and developing cGVHD. FCRL3 gene haplotypes with frequency >0.01 were -TGGG-, -CACA- and -CGCA-. Chronic GVHD patients significantly less the frequency of -CACA- or -CGCA- allele than non GVHD patients (p=0.0040). There were no significant difference in donor allele frequency and incidence of cGVHD. In conclusion, our studies show FCRL3, which is autoimmune disease associated gene, is also the candidate of cGVHD associated gene and its protective haplotype may prevent from occurring cGVHD but not homologous another FCRL proteins.

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Chen, Jianmin, Jasdeep K. Saggar, Paul Corey, and Lilian U. Thompson. "Flaxseed cotyledon fraction reduces tumour growth and sensitises tamoxifen treatment of human breast cancer xenograft (MCF-7) in athymic mice." British Journal of Nutrition 105, no. 3 (December 7, 2010): 339–47. http://dx.doi.org/10.1017/s0007114510003557.

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Dietary flaxseed (FS) inhibited the growth of human breast tumours and enhanced the effectiveness of tamoxifen (TAM) in athymic mice with low oestradiol (E2) levels. The present study determined whether the n-3 fatty acid-rich cotyledon fraction of FS (FC), alone or in combination with TAM, has a similar effect and thus can substitute for FS. In a 2 × 2 factorial design, ovariectomised mice with established oestrogen receptor (ER)-positive breast tumours (MCF-7) were treated as follows: groups 1 and 2 were fed the basal diet (BD, control) and FC diet (82 g FC/kg), respectively. Groups 3 and 4 with TAM implants (5 mg) were fed the BD and FC diet, respectively. At 8 weeks post-treatment, mice were euthanised, and tumours were analysed by immunohistochemistry and real-time PCR. BD, FC and FC/TAM groups significantly decreased tumour area, but the TAM group did not. Tumour regression in the FC/TAM group was greater compared to the TAM group. FC lowered cell proliferation but had no effect on apoptosis; the opposite was observed with TAM. FC suppressed mRNA expressions of pS2 and insulin-like growth factor 1 receptor (IGF-1R) and protein expressions of ERα, phosphospecific ERα, human epidermal growth factor receptor 2 (HER2), phosphospecific HER2 (pHER2) and amplified in breast 1 (AIB1), while TAM up-regulated mRNA expressions of Bcl2, progesterone receptor and IGF-1R and protein expression of pHER2, and down-regulated ERβ mRNA. FC modulated the effect of TAM on tumour growth biomarkers. In conclusion, FC reduced the growth of ER+human breast tumours at low circulating E2, alone and combined with TAM, in part through modulation of ER − and growth factor-mediated signalling pathways; it may substitute for FS in increasing the effectiveness of TAM.

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Terrier, Benjamin, Satoshi Nagata, Tomoko Ise, Michelle Rosenzwajg, Ira Pastan, David Klatzmann, David Saadoun, and Patrice Cacoub. "CD21−/lowMarginal Zone B Cells Highly Express Fc Receptor-like 5 Protein and Are Killed by Anti-Fc Receptor-like 5 Immunotoxins in Hepatitis C Virus-Associated Mixed Cryoglobulinemia Vasculitis." Arthritis & Rheumatology 66, no. 2 (January 27, 2014): 433–43. http://dx.doi.org/10.1002/art.38222.

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Li, Huifang, Francisco Borrego, Satoshi Nagata, and Mate Tolnay. "Fc Receptor–like 5 Expression Distinguishes Two Distinct Subsets of Human Circulating Tissue–like Memory B Cells." Journal of Immunology 196, no. 10 (April 13, 2016): 4064–74. http://dx.doi.org/10.4049/jimmunol.1501027.

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Weinshank, R. L., A. D. Luster, and J. V. Ravetch. "Function and regulation of a murine macrophage-specific IgG Fc receptor, Fc gamma R-alpha." Journal of Experimental Medicine 167, no. 6 (June 1, 1988): 1909–25. http://dx.doi.org/10.1084/jem.167.6.1909.

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Ligand binding specificities of two cloned murine Fc gamma Rs (Fc gamma R-alpha, Fc gamma R-beta [9]) were determined by gene transfer into Fc gamma R negative cell lines. Both receptors were expressed as full-length molecules capable of IgG immune complex binding that was inhibitable by the mAb 2.4G2. The ligand binding profiles of these receptors were indistinguishable whereby both bound immune-complexed mouse IgG1, IgG2a, and IgG2b, but not IgG3. Neither receptor could bind monomeric IgG2a, indicating these receptors to be low-affinity IgG Fc receptors. Accumulation of the Fc gamma R-alpha mRNA can be induced with murine IFN-gamma at a concentration of 200 U/ml in the macrophage-like cell lines RAW 264.7 and J774a. The time course for induction indicates that the mRNA accumulation is transient but does not return to the uninduced level even after 50 h of treatment. Fc gamma R-beta mRNA was not induced by IFN-gamma, rather its expression was down modulated in mouse peritoneal macrophages. Both RAW and J774a cells lines exhibited increased receptor levels after IFN-gamma stimulation as measured by 125I-2.4G2 and ligand binding. In the absence of IFN-gamma, the RAW and J774a cell lines were minimally phagocytic, while P388D1 cells were actively phagocytic. In the presence of IFN-gamma, however, RAW 264.7 and J774a cells were induced to become actively phagocytic. Induction of Fc gamma R-alpha mRNA and protein by IFN-gamma may be part of the process by which macrophages become activated to engulf antibody-coated particles.

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Shabani, Mahdi, Ali Ahmad Bayat, Mahmood Jeddi-Tehrani, Hodjatallah Rabbani, Mohammad Hojjat-Farsangi, Cristina Ulivieri, Zahra Amirghofran, Cosima Tatiana Baldari, and Fazel Shokri. "Ligation of human Fc receptor like-2 by monoclonal antibodies down-regulates B-cell receptor-mediated signalling." Immunology 143, no. 3 (October 2, 2014): 341–53. http://dx.doi.org/10.1111/imm.12311.

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Yung, Lisa Y., Karl W. K. Tsim, Gang Pei, and Yung H. Wong. "Immunoglobulin G1 Fc Fragment-Tagged Human Opioid Receptor-Like Receptor Retains the Ability to Inhibit cAMP Accumulation." Neurosignals 9, no. 5 (2000): 240–47. http://dx.doi.org/10.1159/000014645.

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PLEASS, Richard J., Paul D. ANDREWS, Michael A. KERR, and Jenny M. WOOF. "Alternative splicing of the human IgA Fc receptor CD89 in neutrophils and eosinophils." Biochemical Journal 318, no. 3 (September 15, 1996): 771–77. http://dx.doi.org/10.1042/bj3180771.

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Receptors for the Fc portion of IgA (FcαR) trigger important immunological elimination processes against IgA-coated targets. Investigation of human FcαR (CD89) transcripts in neutrophils, eosinophils and a monocyte-like cell line, THP-1, with the use of reverse transcriptase PCR, Northern blotting and RNase protection analysis, has provided evidence in these cell types for at least two distinct transcripts generated by alternative splicing. The cDNAs derived from the two major transcripts of both neutrophils and eosinophils have been cloned and sequenced. For both cell types, the larger clone represents the previously described full-length receptor, whereas the second, shorter, splice variant lacks the entire second, membrane-proximal, Ig-like domain. Stable CHO-K1 transfectants have been obtained for both full-length and truncated variant neutrophil receptors. Whereas the full-length receptor is recognized by a panel of five anti-FcαR monoclonal antibodies (mAbs), the shorter variant is bound weakly by only two of the antibodies, suggesting that the epitopes recognized by the majority of the mAbs lie at least in part in the second Ig-like domain of FcαR. Both full-length and splice variant forms of the receptor bind secretory IgA, but the weak binding to serum IgA seen with the full-length receptor is not evident with the shorter variant. Alternative splicing might therefore serve as a means of diversifying FcαR structure and function.

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Cruz, Luis J., Paul J. Tacken, Johan M. S. van der Schoot, Felix Rueda, Ruurd Torensma, and Carl G. Figdor. "ICAM3-Fc Outperforms Receptor-Specific Antibodies Targeted Nanoparticles to Dendritic Cells for Cross-Presentation." Molecules 24, no. 9 (May 12, 2019): 1825. http://dx.doi.org/10.3390/molecules24091825.

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Optimal targeting of nanoparticles (NP) to dendritic cells (DCs) receptors to deliver cancer-specific antigens is key to the efficient induction of anti-tumour immune responses. Poly (lactic-co-glycolic acid) (PLGA) nanoparticles containing tètanus toxoid and gp100 melanoma-associated antigen, toll-like receptor adjuvants were targeted to the DC-SIGN receptor in DCs by specific humanized antibodies or by ICAM3-Fc fusion proteins, which acts as the natural ligand. Despite higher binding and uptake efficacy of anti-DC-SIGN antibody-targeted NP vaccines than ICAM3-Fc ligand, no difference were observed in DC activation markers CD80, CD83, CD86 and CCR7 induced. DCs loaded with NP coated with ICAM3-Fc appeared more potent in activating T cells via cross-presentation than antibody-coated NP vaccines. This fact could be very crucial in the design of new cancer vaccines.

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Ono, Etsuro, Yukiko Tomioka, Yuki Watanabe, Keiko Amagai, Masami Morimatsu, Kyoko Shinya, and Pierre Cherel. "Comparison of the antiviral potentials among the pseudorabies-resistant transgenes encoding different soluble forms of porcine nectin-1 in transgenic mice." Journal of General Virology 88, no. 10 (October 1, 2007): 2636–41. http://dx.doi.org/10.1099/vir.0.83080-0.

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Nectin-1 is an alphaherpesvirus receptor that binds to virion glycoprotein D by the first immunoglobulin (Ig)-like domain. The possibility of making animals resistant to pseudorabies virus (PRV) infection has been investigated by generating transgenic mice expressing soluble forms of porcine nectin-1. Previously, transgenic mice were generated that expressed a fusion protein made of the entire ectodomain of nectin-1 fused to the Fc portion of human IgG, or the first Ig-like domain fused to the Fc portion of porcine IgG. Here, the contribution of the second and third Ig-like domains of nectin-1 was analysed by generating transgenic mice expressing the entire ectodomain of nectin-1 fused to the porcine Fc portion. Transgenic mice expressing each of three different fusion proteins were challenged with PRV for comparison of their resistance. Altogether, mice transgenic for a chimera that carried the entire ectodomain were more resistant than those transgenic for a chimera that carried the first Ig-like domain.

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Sang, Daoqian, Qiming Chen, Xiaolin Liu, Hongdang Qu, Daoxiang Wei, Liang Yin, and Lina Zhang. "Fc receptor like 3 in Chinese patients of Han nationality with Guillain–Barré syndrome." Journal of Neuroimmunology 246, no. 1-2 (May 2012): 65–68. http://dx.doi.org/10.1016/j.jneuroim.2012.03.006.

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Umemura, T. "Genetic association of Fc receptor-like 3 polymorphisms with autoimmune pancreatitis in Japanese patients." Gut 55, no. 9 (September 1, 2006): 1367–68. http://dx.doi.org/10.1136/gut.2006.095059.

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Fernandez-Vizarra, P., O. Lopez-Franco, B. Mallavia, A. Higuera-Matas, V. Lopez-Parra, G. Ortiz-Munoz, E. Ambrosio, J. Egido, O. F. X. Almeida, and C. Gomez-Guerrero. "Immunoglobulin G Fc receptor deficiency prevents Alzheimer-like pathology and cognitive impairment in mice." Brain 135, no. 9 (September 1, 2012): 2826–37. http://dx.doi.org/10.1093/brain/aws195.

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Wilson, Ian A., and Pamela J. Bjorkman. "Unusual MHC-like molecules; CD1, Fc receptor, the hemochromatosis gene product, and viral homologs." Current Opinion in Immunology 10, no. 1 (February 1998): 67–73. http://dx.doi.org/10.1016/s0952-7915(98)80034-4.

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Rostamzadeh, Davood, Tohid Kazemi, Zahra Amirghofran, and Mahdi Shabani. "Update on Fc receptor-like (FCRL) family: new immunoregulatory players in health and diseases." Expert Opinion on Therapeutic Targets 22, no. 6 (May 10, 2018): 487–502. http://dx.doi.org/10.1080/14728222.2018.1472768.

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Haga, C. L., G. R. A. Ehrhardt, R. J. Boohaker, R. S. Davis, and M. D. Cooper. "Fc receptor-like 5 inhibits B cell activation via SHP-1 tyrosine phosphatase recruitment." Proceedings of the National Academy of Sciences 104, no. 23 (May 23, 2007): 9770–75. http://dx.doi.org/10.1073/pnas.0703354104.

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Agarwal, Stuti, Zachary Kraus, Jessica Dement-Brown, Oyeleye Alabi, Kyle Starost, and Mate Tolnay. "Human Fc Receptor-like 3 Inhibits Regulatory T Cell Function and Binds Secretory IgA." Cell Reports 30, no. 5 (February 2020): 1292–99. http://dx.doi.org/10.1016/j.celrep.2019.12.099.

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Lee, Young Ho, Jin-Hyun Woo, Seong Jae Choi, Jong Dae Ji, and Gwan Gyu Song. "Fc receptor-like 3 −169 C/T polymorphism and RA susceptibility: a meta-analysis." Rheumatology International 30, no. 7 (August 19, 2009): 947–53. http://dx.doi.org/10.1007/s00296-009-1082-5.

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Jirapongpairoj, Walissara, Ikuo Hirono, and Hidehiro Kondo. "Identification and expression analysis of Fc receptor-like proteins in Japanese flounder (Paralichthys olivaceus)." Fish & Shellfish Immunology 87 (April 2019): 82–86. http://dx.doi.org/10.1016/j.fsi.2019.01.002.

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Rozsnyay, Z., G. Sármay, I. Szabó, Gy Medgyesi, G. Gorini, and J. Gergely. "Fine specificity of a rabbit antibody interacting with human IgG Fc receptor-like molecules." Immunology Letters 25, no. 4 (September 1990): 303–11. http://dx.doi.org/10.1016/0165-2478(90)90200-a.

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Raab, Stefanie, Julia Steinbacher, Ludger Grosse-Hovest, Benjamin J. Schmiedel, Alexander Steinle, Lothar Kanz, and Helmut R. Salih. "Induction of NK Cell Reactivity in Breast Cancer by Fc-Engineered NKG2D-Ig Fusion Proteins." Blood 120, no. 21 (November 16, 2012): 253. http://dx.doi.org/10.1182/blood.v120.21.253.253.

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Abstract Abstract 253 NK cells are cytotoxic lymphocytes that play an important role in anti-tumor immunity. Their capability to mediate Fc-receptor dependent effector functions like antibody dependent cellular cytotoxicity (ADCC) largely contributes to the clinical success of anti-tumor antibodies like Herceptin (Trastuzumab®), which is approved for treatment of breast cancer displaying HER2/neu-overexpression. Notably, only about 20% of breast cancer patients show overexpression of HER2/neu. Moreover, this antigen is also expressed on healthy cells, and application of Herceptin is associated with side effects. In contrast, ligands of the activating immunoreceptor NKG2D (NKG2DL) are widely expressed on malignant cells, but generally absent on healthy tissues. We aimed to take advantage of the tumor-restricted expression of NKG2DL by using them as tumor-antigens for Fc-optimized NKG2D-Ig fusion proteins targeting breast cancer cells for NK cell ADCC and IFN-γ production. NKG2D-Ig fusion proteins with distinct modifications in their Fc portion were generated by amino acid exchange as previously described (Lazar 2006; Armour 1999). Compared to wildtype NKG2D-Fc (NKG2D-Fc-WT) or Herceptin, our mutants (S239D/I332E and E233P/L234V/L235A/ΔG236/A327G/A330S) displayed highly enhanced (NKG2D-Fc-ADCC) and abrogated (NKG2D-Fc-KO) affinity to the NK cell FcγRIIIa receptor (CD16), respectively. This resulted in lacking (NKG2D-Fc-KO) or highly enhanced (NKG2D-Fc-ADCC) NK cell activation. In cultures of NK cells and breast cancer cells, NKG2D-Fc-KO significantly reduced NK cell reactivity due to blockade of NKG2DL-mediated activating signals, while NKG2D-Fc-WT substantially enhanced NK reactivity by induction of ADCC and cytokine production. Notably, the effect of our NKG2D-Fc-ADCC by far exceeded that of NKG2D-Fc-WT and, in case of HER2/neu low targets, also that of Herceptin, resulting in potently enhanced NK anti-tumor reactivity. Together, our results demonstrate that Fc-engineered NKG2D-Fc-ADCC fusion proteins can effectively target NKG2DL-expressing cancer cells for NK anti-tumor reactivity. In line with the hierarchically organized potential of the various activating receptors governing NK reactivity and due to its highly increased affinity to CD16 NKG2D-Fc-ADCC potently enhances NK cell reactivity despite the inevitable reduction of activating signals upon binding to NKG2DL. Due to the tumor-restricted expression of NKG2DL, NKG2D-Fc-ADCC may thus constitute an attractive means for immunotherapy, especially of HER2/neu-low or -negative breast cancer. Disclosures: No relevant conflicts of interest to declare.

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Kubagawa, Hiromi, Christopher M. Skopnik, Khlowd Al-Qaisi, Rosaleen A. Calvert, Kazuhito Honjo, Yoshiki Kubagawa, Ruth Teuber, et al. "Differences between Human and Mouse IgM Fc Receptor (FcµR)." International Journal of Molecular Sciences 22, no. 13 (June 29, 2021): 7024. http://dx.doi.org/10.3390/ijms22137024.

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Both non-immune “natural” and antigen-induced “immune” IgM are important for protection against pathogens and for regulation of immune responses to self-antigens. Since the bona fide IgM Fc receptor (FcµR) was identified in humans by a functional cloning strategy in 2009, the roles of FcµR in these IgM effector functions have begun to be explored. In this short essay, we describe the differences between human and mouse FcµRs in terms of their identification processes, cellular distributions and ligand binding activities with emphasis on our recent findings from the mutational analysis of human FcµR. We have identified at least three sites of human FcµR, i.e., Asn66 in the CDR2, Lys79 to Arg83 in the DE loop and Asn109 in the CDR3, responsible for its constitutive IgM-ligand binding. Results of computational structural modeling analysis are consistent with these mutational data and a model of the ligand binding, Ig-like domain of human FcµR is proposed. Serendipitously, substitution of Glu41 and Met42 in the CDR1 of human FcµR with mouse equivalents Gln and Leu, either single or more prominently in combination, enhances both the receptor expression and IgM binding. These findings would help in the future development of preventive and therapeutic interventions targeting FcµR.

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Jin, Ming-hao, Kazunobu Sawamoto, Mikiko Ito, and Hideyuki Okano. "The Interaction between the DrosophilaSecreted Protein Argos and the Epidermal Growth Factor Receptor Inhibits Dimerization of the Receptor and Binding of Secreted Spitz to the Receptor." Molecular and Cellular Biology 20, no. 6 (March 15, 2000): 2098–107. http://dx.doi.org/10.1128/mcb.20.6.2098-2107.2000.

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ABSTRACT Drosophila Argos (Aos), a secreted protein with an epidermal growth factor (EGF)-like domain, has been shown to inhibit the activation of the Drosophila EGF receptor (DER). However, it has not been determined whether Aos binds directly to DER or whether regulation of the DER activation occurs through some other mechanism. Using DER-expressing cells (DER/S2) and a recombinant DER extracellular domain-Fc fusion protein (DER-Fc), we have shown that Aos binds directly to the extracellular domain of DER with its carboxyl-terminal region, including the EGF-like domain. Furthermore, Aos can block the binding of secreted Spitz (sSpi), a transforming growth factor α-like ligand of DER, to the extracellular domain of DER. We observed that sSpi stimulates the dimerization of both the soluble DER extracellular domain (sDER) and the intact DER in the DER/S2 cells and that Aos can block the sSpi-induced dimerization of both sDER and intact DER. Moreover, we have shown that, by directly interacting with DER, Aos and SpiAos (a chimeric protein that is composed of the N-terminal region of Spi and the C-terminal region of Aos) inhibit the dimerization and phosphorylation of DER that are induced by DER's overexpression in the absence of sSpi. These results indicate that Aos exerts its inhibitory function through dual molecular mechanisms: by blocking both the receptor dimerization and the binding of activating ligand to the receptor. This is the first description of this novel inhibitory mechanism for receptor tyrosine kinases.

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Kubagawa, Hiromi, Satoshi Oka, Yoshiki Kubagawa, Ikuko Torii, Eiji Takayama, Dong-Won Kang, G. Larry Gartland, et al. "Identity of the elusive IgM Fc receptor (FcμR) in humans." Journal of Experimental Medicine 206, no. 12 (October 26, 2009): 2779–93. http://dx.doi.org/10.1084/jem.20091107.

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Although Fc receptors (FcRs) for switched immunoglobulin (Ig) isotypes have been extensively characterized, FcR for IgM (FcμR) has defied identification. By retroviral expression and functional cloning, we have identified a complementary DNA (cDNA) encoding a bona fide FcμR in human B-lineage cDNA libraries. FcμR is defined as a transmembrane sialoglycoprotein of ∼60 kD, which contains an extracellular Ig-like domain homologous to two other IgM-binding receptors (polymeric Ig receptor and Fcα/μR) but exhibits an exclusive Fcμ-binding specificity. The cytoplasmic tail of FcμR contains conserved Ser and Tyr residues, but none of the Tyr residues match the immunoreceptor tyrosine-based activation, inhibitory, or switch motifs. Unlike other FcRs, the major cell types expressing FcμR are adaptive immune cells, including B and T lymphocytes. After antigen-receptor ligation or phorbol myristate acetate stimulation, FcμR expression was up-regulated on B cells but was down-modulated on T cells, suggesting differential regulation of FcμR expression during B and T cell activation. Although this receptor was initially designated as Fas apoptotic inhibitory molecule 3, or TOSO, our results indicate that FcμR per se has no inhibitory activity in Fas-mediated apoptosis and that such inhibition is only achieved when anti-Fas antibody of an IgM but not IgG isotype is used for inducing apoptosis.

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Blázquez-Moreno, Alfonso, Soohyung Park, Wonpil Im, Melissa J. Call, Matthew E. Call, and Hugh T. Reyburn. "Transmembrane features governing Fc receptor CD16A assembly with CD16A signaling adaptor molecules." Proceedings of the National Academy of Sciences 114, no. 28 (June 26, 2017): E5645—E5654. http://dx.doi.org/10.1073/pnas.1706483114.

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Many activating immunoreceptors associate with signaling adaptor molecules like FcεR1γ or CD247. FcεR1γ and CD247 share high sequence homology and form disulphide-linked homodimers that contain a pair of acidic aspartic acid residues in their transmembrane (TM) domains that mediate assembly, via interaction with an arginine residue at a similar register to these aspartic acids, with the activating immunoreceptors. However, this model cannot hold true for receptors like CD16A, whose TM domains do not contain basic residues. We have carried out an extensive site-directed mutagenesis analysis of the CD16A receptor complex and now report that the association of receptor with the signaling adaptor depends on a network of polar and aromatic residues along the length of the TM domain. Molecular modeling indicates that CD16A TM residues F202, D205, and T206 form the core of the membrane-embedded trimeric interface by establishing highly favorable contacts to the signaling modules through rearrangement of a hydrogen bond network previously identified in the CD247 TM dimer solution NMR structure. Strikingly, the amino acid D205 also regulates the turnover and surface expression of CD16A in the absence of FcεR1γ or CD247. Modeling studies indicate that similar features underlie the association of other activating immune receptors, including CD64 and FcεR1α, with signaling adaptor molecules, and we confirm experimentally that equivalent F, D, and T residues in the TM domain of FcεR1α markedly influence the biology of this receptor and its association with FcεR1γ.

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Sprague, Elizabeth R., Henrike Reinhard, Evelyn J. Cheung, Alexander H. Farley, Robin Deis Trujillo, Hartmut Hengel, and Pamela J. Bjorkman. "The Human Cytomegalovirus Fc Receptor gp68 Binds the Fc CH2-CH3 Interface of Immunoglobulin G." Journal of Virology 82, no. 7 (January 23, 2008): 3490–99. http://dx.doi.org/10.1128/jvi.01476-07.

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ABSTRACT Recognition of immunoglobulin G (IgG) by surface receptors for the Fc domain of immunoglobulin G (Fcγ), FcγRs, can trigger both humoral and cellular immune responses. Two human cytomegalovirus (HCMV)-encoded type I transmembrane receptors with Fcγ-binding properties (vFcγRs), gp34 and gp68, have been identified on the surface of HCMV-infected cells and are assumed to confer protection against IgG-mediated immunity. Here we show that Fcγ recognition by both vFcγRs occurs independently of N-linked glycosylation of Fcγ, in contrast with the properties of host FcγRs. To gain further insight into the interaction with Fcγ, truncation mutants of the vFcγR gp68 ectodomain were probed for Fcγ binding, resulting in localization of the Fcγ binding site on gp68 to residues 71 to 289, a region including an immunoglobulin-like domain. Gel filtration and biosensor binding experiments revealed that, unlike host FcγRs but similar to the herpes simplex virus type 1 (HSV-1) Fc receptor gE-gI, gp68 binds to the CH2-CH3 interdomain interface of the Fcγ dimer with a nanomolar affinity and a 2:1 stoichiometry. Unlike gE-gI, which binds Fcγ at the slightly basic pH of the extracellular milieu but not at the acidic pH of endosomes, the gp68/Fcγ complex is stable at pH values from 5.6 to pH 8.1. These data indicate that the mechanistic details of Fc binding by HCMV gp68 differ from those of host FcγRs and from that of HSV-1 gE-gI, suggesting distinct functional and recognition properties.

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van Lent, P. L. E. M., A. B. Blom, L. Grevers, A. Sloetjes, and W. B. van den Berg. "Toll-like receptor 4 induced Fc R expression potentiates early onset of joint inflammation and cartilage destruction during immune complex arthritis: Toll-like receptor 4 largely regulates Fc R expression by interleukin 10." Annals of the Rheumatic Diseases 66, no. 3 (March 1, 2007): 334–40. http://dx.doi.org/10.1136/ard.2006.057471.

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Shabani, Mahdi, Azam Hemmati, Mahdi Zandemami, Jalal Khoshnoodi, Mahmood Jeddi-Tehrani, Hodjatallah Rabbani, Zahra Amirghofran, and Fazel Shokri. "Cloning, Expression and Characterization of Recombinant Human Fc Receptor Like 1, 2 and 4 Molecules." Iranian Journal of Biotechnology 11, no. 3 (August 1, 2013): 182–92. http://dx.doi.org/10.5812/ijb.9950.

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Zhao, Xingwang, Hengyi Xie, Meng Zhao, Asma Ahsan, Xinxin Li, Fei Wang, Junyang Yi, et al. "Fc receptor–like 1 intrinsically recruits c-Abl to enhance B cell activation and function." Science Advances 5, no. 7 (July 2019): eaaw0315. http://dx.doi.org/10.1126/sciadv.aaw0315.

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B cell activation is regulated by the stimulatory or inhibitory co-receptors of B cell receptors (BCRs). Here, we investigated the signaling mechanism of Fc receptor-like 1 (FcRL1), a newly identified BCR co-receptor. FcRL1 was passively recruited into B cell immunological synapses upon BCR engagement in the absence of FcRL1 cross-linking, suggesting that FcRL1 may intrinsically regulate B cell activation and function. BCR cross-linking alone led to the phosphorylation of the intracellular Y281ENV motif of FcRL1 to provide a docking site for c-Abl, an SH2 domain-containing kinase. The FcRL1 and c-Abl signaling module, in turn, potently augmented B cell activation and proliferation. FcRL1-deficient mice exhibited markedly impaired formation of extrafollicular plasmablasts and germinal centers, along with decreased antibody production upon antigen stimulation. These findings reveal a critical BCR signal-enhancing function of FcRL1 through its intrinsic recruitment to B cell immunological synapses and subsequent recruitment of c-Abl upon BCR cross-linking.

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Journal articles on the topic 'Fc receptor-like'

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