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首页> 外文期刊>European Journal of Cell Biology: Journal of Deutsche Gesellschaft fur Elektronenmikroskopie: Journal of Deutsche Gesellschaft fur Zellbiologie >Parafusin is a membrane and vesicle associated protein that cycles atexocytosis
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Parafusin is a membrane and vesicle associated protein that cycles atexocytosis

机译：副夫黄素是一种膜和囊泡相关蛋白，可循环发生胞吐作用

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摘要

In the unicellular eukaryote Paramecium tetraurelia, stimulation of exocytosis leads to Ca2+ activation of an alpha Glc-1-phosphodiesterase that dephosphoglucosylates the phosphoglycoprotein parafusin (PFUS), This process fails in exo(.) mutant nd9 and also in the absence of Ca2+ influx upon stimulation suggesting that PFUS dephosphoglucosylation may be causally related to exocytosis. To further corroborate the hypothesis that PFUS is involved in the molecular events in egocytosis, we used laser confocal scanning microscopy and a PFUS specific peptide antibody to perform localization studies of PFUS in wild type (wt) and mutant Paramecium. In unstimulated wt cells, PLUS was associated both with the exocytic site of the cell membrane and with the membrane of the dense core secretory vesicles. Localization at these two sites was shown to be independent of each other since the exocytosis mutant (exo(.)) tam8, in which docking of its vesicles is blocked, still showed cell membrane staining, Immunofluorescence and immunoblotting of isolated intact secretory resides also revealed PFUS association, Upon stimulation of exocytosis, PLUS dissociated from both the dense core secretory vesicles and the cell membrane in a Ca2+-dependent manner, During recovery of exocytic capacity. PLUS reassociated with the newly formed secretory resides in the cytoplasm prior to their docking at the exocytic sites, Immunoblot analysis of PLUS during this time showed no changes in levels of the protein, Stimulation of exocytosis in wt in Mg2+ buffer or in the exo(.) temperature sensitive mutant (nd9) at the non-permissive temperature did not lead to dissociation of the PFUS. We conclude that PFUS is a novel critical component whose cycling probably participates in the molecular exocytic fusion machinery in these cells.
机译：在单细胞真核生物草履虫中，胞吐作用的刺激导致αGlc-1-磷酸二酯酶的Ca2 +活化，从而使磷酸糖蛋白副融合素（PFUS）去磷酸化，该过程在exo（。）突变体nd9中失败，并且在不存在Ca2 +流入时刺激提示PFUS去磷酸葡萄糖基化可能与胞吐作用有因果关系。为了进一步证实PFUS参与细胞吞噬作用的分子假说，我们使用激光共聚焦扫描显微镜和PFUS特异性肽抗体对PFUS在野生型（wt）和突变型草履虫中的定位进行了研究。在未刺激的wt细胞中，PLUS与细胞膜的胞外位点和致密核心分泌囊泡的膜都相关。由于胞吐突变体（exo（。））tam8（其中囊泡的对接被阻断）仍显示细胞膜染色，免疫荧光和分离的完整分泌物残留的免疫印迹，因此显示这两个位点彼此独立。 PFUS协会，在刺激胞吐作用后，在胞外力恢复期间，PLUS以Ca2 +依赖的方式从致密的核心分泌囊泡和细胞膜上解离。与新形成的分泌物重新结合的PLUS在它们停靠在胞外位点之前先存在于细胞质中，在此期间PLUS的免疫印迹分析表明蛋白质水平没有变化，Mg2 +缓冲液或exo（。 ）温度敏感突变体（nd9）在非容许温度下未导致PFUS的解离。我们得出的结论是，PFUS是一种新型的关键成分，其循环可能参与了这些细胞中的分子胞外融合机制。

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