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Most of the fer-1 mutations fall within these C2 domains, showing that they have distinct, non-redundant functions. We found that membranous organelle fusion requires intracellular Ca2+ and that C2 domain mutations alter Ca2+ sensitivity. This suggests that the C2 domains are involved in Ca2+ sensing and further supports their independent function. Using two immunological approaches we found three FER-1 isoforms, two of which might arise from FER-1 by proteolysis. By both light and electron microscopy, these FER-1 proteins were found to be localized to membranous organelle membranes. Dysferlin, a human homologue of FER-1 involved in muscular dystrophy, is required for vesicle fusion during Ca2+-induced muscle membrane repair. Our results suggest that the ferlin family members share a conserved mechanism to regulate cell-type-specific membrane fusion.<\/jats:p>","DOI":"10.1242\/jcs.02980","type":"journal-article","created":{"date-parts":[[2006,5,31]],"date-time":"2006-05-31T08:55:39Z","timestamp":1149065739000},"page":"2552-2562","source":"Crossref","is-referenced-by-count":135,"title":["FER-1 regulates Ca2+-mediated membrane fusion during <i>C. elegans<\/i> spermatogenesis"],"prefix":"10.1242","volume":"119","author":[{"given":"N. L.","family":"Washington","sequence":"first","affiliation":[{"name":"Department of Molecular and Cellular Biology, The University of Arizona, 1007 E. Lowell Street, Life Sciences South 452, Tucson, AZ, 85721, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S.","family":"Ward","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cellular Biology, The University of Arizona, 1007 E. 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