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Two alternatively spliced transcripts, elp-1a and elp-1b, are shown with exons as solid boxes and introns as lines. (A) The physical map of elp-1 is drawn in the reverse orientation. Genetic and molecular characterization of elp-1. These data imply that ELP-1 may play an important role during the transmission of forces and signals between the body surface and both muscle cells and touch receptor neurons. Consistent with this idea, decreasing ELP-1 expression decreases sensitivity to gentle touch applied to the body wall. This restricted localization in the nervous system implies that ELP-1 plays a role in mechanotransmission. ELP-1 is also expressed in a subset of mechanoreceptor neurons, including the ray neurons in the male tail, microtubule-rich touch receptor neurons, and the six ciliated IL1 neurons. In muscle, ELP-1 is associated with adhesion complexes near the cell surface and is bound to a criss-crossing network of microtubules in the cytoplasm. In larvae and adults, ELP-1 is expressed in the body wall, spermatheca and vulval muscles, intestine, and hypodermal seam cells. In embryos, ELP-1 is expressed in the hypodermis. elegans ELP-1 by means of transgenic gene expression in living embryos and adults, and by immunolocalization with an ELP-1-specific antibody in fixed tissues. So far, however, the physiological function of this protein family remains unknown.
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Biochemical studies of sea urchin EMAP and vertebrate EMLs implicate these proteins in the regulation of microtubule stability. The EMAP-like protein family has five members in mammals (EML1 through EML5) and only one in both Drosophila (ELP-1) and C. The founding member of the EMAP-like protein family is the Echinoderm Microtubule-Associated Protein (EMAP), so-named for its abundance in sea urchin, starfish, and sand dollar eggs.