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Papers In Press, published online ahead of print September 7, 2005
CBB, EMBL, Heidelberg 69117
Corresponding Author: knop{at}embl.de
During sporulation and meiosis of budding yeast, a developmental program determines the formation of the new plasma membranes of the spores. This process of prospore membrane (PSM) formation leads to the formation of the meiotic daughter cells, the spores, within the lumen of the mother cell. It is initiated at the spindle pole bodies (SPBs) during meiosis II. Spore formation, but not meiotic cell cycle progression, requires the function of phospholipase D (PLD/Spo14). Here we show that PLD/Spo14 forms a complex with Sma1, a meiotically expressed protein essential for spore formation. Detailed analysis revealed that both proteins are required for early steps of prospore membrane assembly, however with distinct defects in the respective mutants. In the spo14 mutant initiation of PSM formation is blocked and aggregated vesicles of homogenous size are detected at the SPBs. In contrast, initiation of PSM formation does occur in the sma1 mutant but the enlargement of the membrane is impaired. During PSM growth, both, Spo14 and Sma1 do localize to the membrane and localization of Spo14 is independent on Sma1. Biochemical analysis revealed that Sma1 is not necessary for PLD activity per se, and that PLD present in a complex with Sma1 is highly active. Together our results suggest that yeast PLD is involved in two distinct but essential steps during regulated vesicle fusion necessary for the assembly of the membranous encapsulations of the spores.
J. Biol. Chem, 10.1074/jbc.M504244200
Submitted on April 19, 2005
Revised on August 8, 2005
Accepted on September 7, 2005
Differential requirement for phospholipase D/SPO14 and its novel interactor SMA1 for regulation of exocytotic vesicle fusion in yeast meiosis
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