The yeast GRASP Grh1 colocalizes with COPII and is dispensable for organizing the secretory pathway.

The yeast GRASP Grh1 colocalizes with COPII and is dispensable for organizing the secretory pathway.
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DOI:
10.1111/j.1600-0854.2010.01089.x
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发表时间:
2010-09
期刊:
Traffic (Copenhagen, Denmark)
影响因子:
--
通讯作者:
Glick BS
Glick BS
中科院分区:
其他
文献类型:
--
作者:
Levi SK;Bhattacharyya D;Strack RL;Austin JR 2nd;Glick BS

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在哺乳动物细胞中,“高尔基体重组和堆积蛋白”(GRASP)家族与高尔基体堆积有关,但GRASP蛋白更广泛的功能仍不清楚。酿酒酵母含有一个非必需的GRASP同系物,称为Grh 1。而S.酿酒酵母并没有组织成堆栈,因此Grh 1可能的结构作用很难测试。本文研究了Grh 1在S.酿酒酵母和相关酵母巴斯德毕赤酵母中,其具有堆叠的高尔基池。在协议与早期的研究表明,Grh 1与COPII囊泡外壳蛋白相互作用,我们发现,Grh 1与COPII共定位在过渡期ER(tER)网站在这两种酵母。缺失毕赤酵母Grh 1对tER-高尔基体结构没有明显影响。为了验证S.酿酒酵母Grh 1,我们利用观察到的抑制ER输出在S.酿酒酵母产生通常与顺式高尔基体相关的扩大的tER位点。这种tER-高尔基体关联在Grh 1缺失的情况下得以保留。综合数据表明,Grh 1的行为早期的分泌途径,但分泌室的组织是不稳定的。
In mammalian cells, the “Golgi Reassembly and Stacking Protein” (GRASP) family has been implicated in Golgi stacking, but the broader functions of GRASP proteins are still unclear. The yeast Saccharomyces cerevisiae contains a single nonessential GRASP homolog called Grh1. However, Golgi cisternae in S. cerevisiae are not organized into stacks, so a possible structural role for Grh1 has been difficult to test. Here we examined the localization and function of Grh1 in S. cerevisiae and in the related yeast Pichia pastoris, which has stacked Golgi cisternae. In agreement with earlier studies indicating that Grh1 interacts with COPII vesicle coat proteins, we find that Grh1 colocalizes with COPII at transitional ER (tER) sites in both yeasts. Deletion of P. pastoris Grh1 had no obvious effect on the structure of tER-Golgi units. To test the role of S. cerevisiae Grh1, we exploited the observation that inhibiting ER export in S. cerevisiae generates enlarged tER sites that are often associated with the cis-Golgi. This tER-Golgi association was preserved in the absence of Grh1. The combined data suggest that Grh1 acts early in the secretory pathway but is dispensable for the organization of secretory compartments.
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