Abstract
Neuroactive peptides are packaged as proproteins into dense core vesicles or secretory granules, where they are cleaved at dibasic residues by copackaged proprotein convertases. We show here that the<i>Caenorhabditis elegans egl-3</i> gene encodes a protein that is 57% identical to mouse proprotein convertase type 2 (PC2), and we provide evidence that this convertase regulates mechanosensory responses. Nose touch sensitivity (mediated by ASH sensory neurons) is defective in mutants lacking GLR-1 glutamate receptors (GluRs); however, mutations eliminating the<i>egl-3</i> PC2 restored nose touch sensitivity to<i>glr-1</i> GluR mutants. By contrast, body touch sensitivity (mediated by the touch cells) is greatly diminished in<i>egl-3</i> PC2 mutants. Taken together, these results suggest that <i>egl-3</i> PC2-processed peptides normally regulate the responsiveness of <i>C. elegans</i> to mechanical stimuli.
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