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首页> 外文OA文献 >A cycle of Vam7p release from and PtdIns 3-P–dependent rebinding to the yeast vacuole is required for homotypic vacuole fusion
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A cycle of Vam7p release from and PtdIns 3-P–dependent rebinding to the yeast vacuole is required for homotypic vacuole fusion

机译：同型空泡融合需要一个周期从Vam7p释放和PtdIns 3-P依赖性重新结合到酵母液泡的循环

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Vacuole fusion requires a coordinated cascade of priming, docking, and fusion. SNARE proteins have been implicated in the fusion itself, although their precise role in the cascade remains unclear. We now report that the vacuolar SNAP-23 homologue Vam7p is a mobile element of the SNARE complex, which moves from an initial association with the cis-SNARE complex via a soluble intermediate to the docking site. Soluble Vam7p is specifically recruited to vacuoles and can rescue a fusion reaction poisoned with antibodies to Vam7p. Both the recombinant Vam7p PX domain and a FYVE domain construct of human Hrs block the recruitment of Vam7p and vacuole fusion, demonstrating that phosphatidylinositol 3-phosphate is a primary receptor of Vam7p on vacuoles. We propose that the Vam7p cycle is linked to the availability of a lipid domain on yeast vacuoles, which is essential for coordinating the fusion reaction prior to and beyond docking.
机译：液泡融合需要引发，对接和融合的协调级联。尽管它们在级联反应中的确切作用仍不清楚，但SNARE蛋白已经参与了融合本身。现在我们报道液泡SNAP-23同源物Vam7p是SNARE复合物的移动元件，其从与顺式-SNARE复合物的初始缔合通过可溶的中间体到达对接位点。可溶性Vam7p专门募集到液泡，可以挽救被Vam7p抗体中毒的融合反应。重组的Vam7p PX域和人Hrs的FYVE域构建体均阻断Vam7p的募集和液泡融合，表明磷脂酰肌醇3-磷酸酯是液泡上Vam7p的主要受体。我们提出，Vam7p循环与酵母液泡上脂质结构域的可用性有关，这对于协调对接之前和之后的融合反应至关重要。

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