The EGL-3 proprotein convertase regulates mechanosensory responses of Caenorhabditis elegans

Neuroactive peptides are packaged as proproteins into dense core vesicles o r secretory granules, where they are cleaved at dibasic residues by copacka ged proprotein convertases. We show here that the Caenorhabditis elegans eg l-3 gene encodes a protein that is 57% identical to mouse proprotein conver tase type 2 (PC2), and we provide evidence that this convertase regulates m echanosensory responses. Nose touch sensitivity (mediated by ASH sensory ne urons) is defective in mutants lacking GLR-1 glutamate receptors (GluRs); h owever, mutations eliminating the egl-3 PC2 restored nose touch sensitivity to glr-1 GluR mutants. By contrast, body touch sensitivity (mediated by th e touch cells) is greatly diminished in egl-3 PC2 mutants. Taken together, these results suggest that egl-3 PC2-processed peptides normally regulate t he responsiveness of C. elegans to mechanical stimuli.