{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T05:01:46Z","timestamp":1790830906938,"version":"4.1.0"},"reference-count":75,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Immunol."],"abstract":"<jats:sec>\n                    <jats:title>Background<\/jats:title>\n                    <jats:p>The ITAM-containing FcR\u03b3 chain, encoded by FCER1G, non-covalently couples with the immunoglobulin-binding receptors, -- Fc\u03b3RI (CD64), Fc\u03b3RIIIa (CD16), Fc\u03f5RI and Fc\u03b1RI (CD89), -- to initiate intracellular signals and mediate phagocytosis, cytokine production and other functions. While functionally impactful variants have been identified in the ligand-binding alpha-chains of receptors associated with FcR\u03b3, variants in the signal-generating FcR\u03b3 have not been explored. Signal modulation through structural FcR\u03b3 variants would have implications for FcR\u03b3-associated receptors and their role in immune-mediated diseases.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>\n                      We carried out\n                      <jats:italic>in silico<\/jats:italic>\n                      analyses of whole genome DNA sequence databases based on short-read sequencing of ~76, 000 genomes, long-read sequencing of 1132 genomes, whole exome sequences of ~800, 000 participants and RNA transcript databases. We used the hg38 reference genome to identify genomic DNA and cDNA structural variants and Sanger sequencing of cDNAs derived from FcR\u03b3 mRNAs isolated from local participants to confirm ESTs in circulating immune cells. To detect a putative novel alternatively spliced translated protein (AS-FcR\u03b3), we developed isoform-specific monoclonal antibodies to confirm AS-FcR\u03b3 co-immunoprecipitation with and support of receptor \u03b1-chain expression in transfection systems and primary cells. We assessed the function of the AS-FcR\u03b3 isoform by stimulus-induced cytokine production and degranulation.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>In the human genome, insertions, deletions and rearrangements of FCER1G are absent, and with the exception of very rare single nucleotide variants, the FcR\u03b3 protein is monomorphic. Surprisingly, we confirmed that an alternatively spliced (AS) form of FcR\u03b3 message encodes a translated protein (AS-FcR\u03b3) expressed in human myeloid cells. AS-FcR\u03b3 pairs with ligand binding FcR \u03b1-chains. The alternate exon 5\u2019 in AS-FcR\u03b3 creates a novel cytoplasmic domain with a disrupted ITAM motif. Co-immunoprecipitation showed that AS-FcR\u03b3 associates with Fc\u03b1RI in circulating neutrophils and mononuclear cells. A chimeric molecule consisting of the extracellular domain of Fc\u03b1RI fused to the cytoplasmic domain of AS-FcR\u03b3 fails to stimulate cellular degranulation and cytokine production.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusion<\/jats:title>\n                    <jats:p>AS-FcR\u03b3 is an expressed protein that associates with partner alpha-chains but is not signaling competent. It may represent a novel contributory mechanism mitigating the ability of Fc receptors to stimulate cellular signaling in myeloid cells with important implications for host defense and antibody-mediated autoimmune diseases.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.3389\/fimmu.2026.1856092","type":"journal-article","created":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T04:49:38Z","timestamp":1790830178000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":0,"title":["Identification of a novel, expressed, alternatively spliced FCER1G protein that inhibits receptor function"],"prefix":"10.3389","volume":"17","author":[{"given":"Andrew W.","family":"Gibson","sequence":"first","affiliation":[{"name":"Department of Medicine, The University of Alabama at Birmingham","place":["Birmingham, AL, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jianming","family":"Wu","sequence":"additional","affiliation":[{"name":"Department of Veterinary and Biomedical Sciences, University of Minnesota","place":["Minneapolis, MN, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R. Curtis","family":"Hendrickson","sequence":"additional","affiliation":[{"name":"Department of Microbiology, The University of Alabama at Birmingham","place":["Birmingham, AL, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Travis","family":"Ptacek","sequence":"additional","affiliation":[{"name":"Department of Medicine, The University of Alabama at Birmingham","place":["Birmingham, AL, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chaoling","family":"Dong","sequence":"additional","affiliation":[{"name":"Department of Medicine, The University of Alabama at Birmingham","place":["Birmingham, AL, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Charles E.","family":"Breeze","sequence":"additional","affiliation":[{"name":"Occupational and Environmental Epidemiology Branch, National Cancer Institute","place":["Bethesda, MD, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeffrey C.","family":"Edberg","sequence":"additional","affiliation":[{"name":"Department of Medicine, The University of Alabama at Birmingham","place":["Birmingham, AL, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert P.","family":"Kimberly","sequence":"additional","affiliation":[{"name":"Department of Medicine, The University of Alabama at Birmingham","place":["Birmingham, AL, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2026,10,1]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","DOI":"10.1038\/s41584-024-01152-2","article-title":"Systemic lupus erythematosus genetics: insights into pathogenesis and implications for therapy","volume":"20","author":"Ghodke-Puranik","year":"2024","journal-title":"Nat Rev Rheumatol"},{"key":"B2","doi-asserted-by":"publisher","DOI":"10.1126\/science.ady9543","article-title":"Convergence and divergence of individual immune responses over the life course","volume":"389","author":"Metcalf","year":"2025","journal-title":"Science"},{"key":"B3","doi-asserted-by":"publisher","first-page":"275","DOI":"10.1007\/978-3-319-07911-0_13","article-title":"Human FcR polymorphism and disease","volume":"382","author":"Li","year":"2014","journal-title":"Curr Top Microbiol Immunol"},{"key":"B4","doi-asserted-by":"publisher","DOI":"10.3389\/fimmu.2019.02237","article-title":"Genetic variation in low-to-medium-affinity Fcgamma receptors: functional consequences, disease associations, and opportunities for personalized medicine","volume":"10","author":"Nagelkerke","year":"2019","journal-title":"Front Immunol"},{"key":"B5","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1016\/j.ajhg.2017.11.002","article-title":"The expanding landscape of alternative splicing variation in human populations","volume":"102","author":"Park","year":"2018","journal-title":"Am J Hum Genet"},{"key":"B6","doi-asserted-by":"publisher","DOI":"10.1016\/j.molcel.2019.09.017","article-title":"Alternative splicing regulatory networks: functions, mechanisms, and evolution","volume":"76","author":"Ule","year":"2019","journal-title":"Mol Cell"},{"key":"B7","doi-asserted-by":"publisher","DOI":"10.1182\/blood.v90.3.1109.1109_1109_1114","article-title":"Fc gammaRIIIa-158V\/F polymorphism influences the binding of IgG by natural killer cell Fc gammaRIIIa, independently of the Fc gammaRIIIa-48L\/R\/H phenotype","volume":"90","author":"Koene","year":"1997","journal-title":"Blood"},{"key":"B8","doi-asserted-by":"publisher","DOI":"10.1172\/jci114566","article-title":"Fc gamma receptor III on human neutrophils. 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