TFG Promotes Organization of Transitional ER and Efficient Collagen Secretion.
TFG Promotes Organization of Transitional ER and Efficient Collagen Secretion.
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TFG促进了过渡性和有效胶原蛋白分泌的组织。
DOI：
10.1016/j.celrep.2016.04.062
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发表时间：
2016-05-24
期刊：
影响因子：
8.8
通讯作者：
Stephens DJ
中科院分区：
文献类型：
--
作者：
McCaughey J;Miller VJ;Stevenson NL;Brown AK;Budnik A;Heesom KJ;Alibhai D;Stephens DJ
胶原蛋白是动物王国中最丰富的蛋白质。它在发育过程中对于细胞分化和组织形态发生以及在病理过程如纤维化和癌细胞迁移具有根本重要性。然而，我们对前胶原分泌机制的理解仍然有限。在这里，我们表明，TFG组织过渡ER（tER）和ER出口网站（ERES）到更大的结构。TFG的耗尽导致tER元件的分散，所述tER元件保持与作为主要功能性ERES的个体ER-高尔基体中间隔室（ERGIC）相关联。我们表明，TFG是不需要的运输和包装的小可溶性货物，但必须出口的前胶原从ER。因此，我们的工作表明，ERES的结构和功能之间的关键关系和TFG在优化COPII组装前胶原输出的核心作用。TFG需要将过渡性ER组织成更大的结构。TFG耗尽后，ERES保持与ERGIC紧密贴壁，Mini-ERES支持小的可溶性货物的分泌。表明过渡联邦政府需要支持组织的ER出口网站（ERES）到更大的结构。这种高级组织是前胶原有效分泌所必需的。
Collagen is the most abundant protein in the animal kingdom. It is of fundamental importance during development for cell differentiation and tissue morphogenesis as well as in pathological processes such as fibrosis and cancer cell migration. However, our understanding of the mechanisms of procollagen secretion remains limited. Here, we show that TFG organizes transitional ER (tER) and ER exit sites (ERESs) into larger structures. Depletion of TFG results in dispersion of tER elements that remain associated with individual ER-Golgi intermediate compartments (ERGICs) as largely functional ERESs. We show that TFG is not required for the transport and packaging of small soluble cargoes but is necessary for the export of procollagen from the ER. Our work therefore suggests a key relationship between the structure and function of ERESs and a central role for TFG in optimizing COPII assembly for procollagen export. TFG is required to organize transitional ER into larger structures Following depletion of TFG, ERESs remain in close apposition to the ERGIC Mini-ERESs support secretion of small soluble cargo Large ERESs are required for procollagen secretion McCaughey et al. show that TFG is required to support the organization of ER exit sites (ERESs) into larger structures. This higher-order organization is required for efficient secretion of procollagen.