ArticleCell cycle (Georgetown, Tex.)2017
Discovery of a novel splice variant of Fcar (CD89) unravels sequence segments necessary for efficient secretion: A story of bad signal peptides and good ones that nevertheless do not make it.
Article in Cell cycle (Georgetown, Tex.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Anti-SARS-CoV-2 Spike IgA2 Induces Inflammation by Human Macrophages.European journal of immunology · 2025Article
- Variable-heavy (VH) families influencing IgA1&2 engagement to the antigen, FcαRI and superantigen proteins G, A, and L.Scientific reports · 2022Article
- To Plate or to Simply Unfreeze, That Is the Question for Optimal Plasmid Extraction.Journal of biomolecular techniques : JBT · 2021Article
- Perspective: The promises of a holistic view of proteins-impact on antibody engineering and drug discovery.Bioscience reports · 2019Article
- Role of FcαR EC2 region in extracellular membrane localization.Cell cycle (Georgetown, Tex.) · 2018Article
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Authors and funding
8 authors.
Funding
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Abstract
The IgA receptor, Fcar (CD89) consists of 5 sequence segments: 2 segments (S1, S2) forming the potential signal peptide, 2 extracellular EC domains that include the IgA binding site, and the transmembrane and cytoplasmic tail (TM/C) region. Numerous Fcar splice variants have been reported with various combinations of the sequence segments mentioned above. Here, we report a novel splice variant termed variant APD isolated from a healthy volunteer that lacks only the IgA-binding EC1 domain. Despite possessing the complete signal peptide S1+S2, the variant APD is only found in the intracellular space whereas the wild-type variant 1 is efficiently secreted and variant 4 leaks to the extracellular space. Further mutational experiments involving signal peptide replacements, cleavage site modifications, and studies on alternative isoforms demonstrate that despite the completeness of the signal peptide motif, the presence of the EC1 domain is essential for efficient extracellular export.
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