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First published online 30 May 2006
doi: 10.1242/jcs.02980

Journal of Cell Science 119, 2552-2562 (2006)
Published by The Company of Biologists 2006
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Research Article

FER-1 regulates Ca2+-mediated membrane fusion during C. elegans spermatogenesis

N. L. Washington and S. Ward*

Department of Molecular and Cellular Biology, The University of Arizona, 1007 E. Lowell Street, Life Sciences South 452, Tucson, AZ, 85721, USA

* Author for correspondence (e-mail: samward{at}email.arizona.edu)

Accepted 16 March 2006

FER-1 is required for fusion of specialized vesicles, called membranous organelles, with the sperm plasma membrane during Caenorhabditis elegans spermiogenesis. To investigate its role in membranous organelle fusion, we examined ten fer-1 mutations and found that they all cause the same defect in membrane fusion. FER-1 and the ferlin protein family are membrane proteins with four to seven C2 domains. These domains commonly mediate Ca2+-dependent lipid-processing events. 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.

Key words: Membrane fusion, Spermatogenesis, fer-1, Calcium, Membranous organelle, C2 domain


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