Detection of IL‑17 RD/SEF in K562 Human Cell Line by Flow Cytometry. K562 human chronic myelogenous leukemia cell line was stained with Goat Anti-Human|
IL-17 RD/SEF Fluorescein‑conjugated Antigen Affinity-purified Polyclonal Antibody (Catalog # FAB2275F, filled histogram) or isotype control antibody (Catalog # IC108F, open histogram). View our protocol for Staining Membrane-associated Proteins.
Interleukin-17 receptor D (IL-17 RD), also known as SEF (similar expression to FGFs), is a type I transmembrane protein that is found in both the cytoplasm and plasma membrane (1-5). The gene for this protein belongs to a synexpression group originally identified in zebrafish where SEF is expressed along with FGF-3, -8, sprouty-2 (SPRY2) and SPRY4 (6, 7). By alternate splicing, two transcript variants, potentially encoding three protein isoforms, exist. One is a full-length long form, one a shortened form that uses an alternate start site, and one an alternate splice form that removes the classic signal sequence (1-4). These isoforms have different expression patterns, subcellular localization, and function. The membrane-bound long form of human IL-17RD is synthesized as a 739 amino acid (aa) precursor protein with a putative 27 aa signal peptide, a 272 aa extracellular domain, a 20 aa transmembrane segment and a 420 aa cytoplastic domain. The extracellular domain contains one Ig-like domain and a fibronectin type III motif. The cytoplasmic domain shares homology with the intracellular domains of IL-17 receptor family members and shows one TIR (Toll/IL-1 Receptor) domain and a putative TRAF6-binding motif (2). Natural IL-17 RD has been shown to form homomultimeric complexes (3). Unlike the alternate splice form of IL-17 RD that has a restricted pattern of expression, the full-length IL-17 RD isoform is expressed in most adult tissues and during embryonic development (3, 5). Functionally, IL-17 RD has been shown to be an inhibitor of FGF signaling. The molecule’s extracellular domain does not seem to be involved. There is an interaction between the intracellular domains of FGFR1/2 and IL-17 RD that blocks ERK dissociation from MEK, thereby interfering with downstream ERK activation of nuclear Elk-1 (8). IL-17 RD has also been reported to interact with TAK1 and induce JNK activation and apoptosis (9). Ligands that interact with the extracellular domain of IL-17 RD have not been identified.
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