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First published online March 22, 2006
doi: 10.1242/10.1242/jcs.02841
Research Article |
1 Department of Biochemistry and Cell Biology, SUNY Stony Brook, Stony Brook, NY 4-5215, USA
2 Section of Molecular and Cellular Biology, UC Davis, Davis, CA 95616, USA
3 Boulder Laboratory for 3D Electron Microscopy of Cells, University of Colorado, Boulder, CO 80309, USA
* Author for correspondence (e-mail: Aaron.Neiman{at}sunysb.edu)
Accepted 16 December 2005
Spore formation in Saccharomyces cerevisiae requires the de novo formation of prospore membranes. The coalescence of secretory vesicles into a membrane sheet occurs on the cytoplasmic surface of the spindle pole body. Spo14p, the major yeast phospholipase D, is necessary for prospore membrane formation; however, the specific function of Spo14p in this process has not been elucidated. We report that loss of Spo14p blocks vesicle fusion, leading to the accumulation of prospore membrane precursor vesicles docked on the spindle pole body. A similar phenotype was seen when the t-SNARE Sso1p, or the partially redundant t-SNAREs Sec9p and Spo20p were mutated. Although phosphatidic acid, the product of phospholipase D action, was necessary to recruit Spo20p to the precursor vesicles, independent targeting of Spo20p to the membrane was not sufficient to promote fusion in the absence of SPO14. These results demonstrate a role for phospholipase D in vesicle fusion and suggest that phospholipase D-generated phosphatidic acid plays multiple roles in the fusion process.
Key words: Sporulation, Prospore membrane, Vesicle fusion, SNARE, Phospholipase D
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