Biogenesis of a novel compartment for autophagosome-mediated unconventional protein secretion.
Biogenesis of a novel compartment for autophagosome-mediated unconventional protein secretion.
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DOI：
10.1083/jcb.201106098
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发表时间：
2011-12-12
期刊：
影响因子：
--
通讯作者：
Malhotra V
中科院分区：
文献类型：
--
作者：
Bruns C;McCaffery JM;Curwin AJ;Duran JM;Malhotra V
一种称为CUPS的新型膜结构在非常规货物如Acb 1的分泌过程中组装。Acb 1的内质网（ER）-高尔基体独立的非常规分泌需要许多不同的蛋白质。它们包括自噬体形成所必需的蛋白质，膜与内体融合所必需的蛋白质，多泡体途径的蛋白质，以及细胞表面靶膜SNARE Sso 1，从而提出了这些不同蛋白质与Acb 1分泌之间的联系的问题。在本研究中，我们现在报告说，饥饿后，在酿酒酵母，Grh 1收集到独特的膜结构附近的Sec 13含ER出口站点。磷脂酰肌醇3磷酸，ESCRT（运输所需的内体分选复合物）蛋白Vps 23，和自噬相关蛋白Atg 8和Atg 9被招募到这些含有Grh 1的膜，缺乏高尔基体和内体的成分，我们称之为非常规蛋白分泌（CUPS）的新隔室。我们描述了CUPS的生物发生所需的细胞蛋白，我们认为这是Acb 1从细胞中释放的分选站。
A novel membrane structure called CUPS is assembled during the secretion of unconventional cargo such as Acb1. The endoplasmic reticulum (ER)–Golgi-independent, unconventional secretion of Acb1 requires many different proteins. They include proteins necessary for the formation of autophagosomes, proteins necessary for the fusion of membranes with the endosomes, proteins of the multivesicular body pathway, and the cell surface target membrane SNARE Sso1, thereby raising the question of what achieves the connection between these diverse proteins and Acb1 secretion. In the present study, we now report that, upon starvation in Saccharomyces cerevisiae, Grh1 is collected into unique membrane structures near Sec13-containing ER exit sites. Phosphatidylinositol 3 phosphate, the ESCRT (endosomal sorting complex required for transport) protein Vps23, and the autophagy-related proteins Atg8 and Atg9 are recruited to these Grh1-containing membranes, which lack components of the Golgi apparatus and the endosomes, and which we call a novel compartment for unconventional protein secretion (CUPS). We describe the cellular proteins required for the biogenesis of CUPS, which we believe is the sorting station for Acb1’s release from the cells.
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影响因子：
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作者：
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DOI：
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发表时间：
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期刊：
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