2024/10/15
paper · doi:10.17912/micropub.biology.001374
<p>Fibroblast Growth Factor Receptors (FGFRs) play a role in diverse developmental pathways that mediate cell proliferation, cell migration, and cell survival. We use <i><a href="https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=6239" id="afe3aa58-2cd7-42e1-ae77-6cddca9fee55">C. elegans</a></i> as a model to better understand FGFR signaling specificity. <i><a href="https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=6239" id="d6cdcfb0-4bf2-46f1-b9a8-7444f0684d17">C. elegans</a></i> has a single FGFR, <a href="http://www.wormbase.org/db/get?name=WBGene00001184;class=Gene" id="dff04def-410a-4a7f-9a9e-dfcca4ba2c67">EGL-15</a>. <a href="http://www.wormbase.org/db/get?name=WBGene00001184;class=Gene" id="698abefc-f864-4d1c-8523-d649bbaab524">EGL-15</a> contains an alternatively spliced exon 5 that results in two isoforms, <a>EGL-15</a>(5A) and <a>EGL-15</a>(5B), that differ in their extracellular domains. The <a>EGL-15</a>(5A) isoform is required for the chemoattraction of a pair of migrating sex myoblasts, whose correct positioning is required for egg laying. Deletion of the 5A domain results in an egg-laying defective (Egl) organism. We identified six highly conserved amino acids within the 5A domain and found that two amino acids, S145 and L148 are specifically required for sex myoblast migration in <i><a href="https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=6239" id="afc679bc-16f2-44e0-8187-5c109eaee066">C. elegans</a></i>.</p>