Exomer: A coat complex for transport of select membrane proteins from the trans-Golgi network to the plasma membrane in yeast.
Exomer: A coat complex for transport of select membrane proteins from the trans-Golgi network to the plasma membrane in yeast.
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EXOMER：一种用于将精选膜蛋白从反式高尔基网络转移到酵母中质膜的外套复合物。
DOI：
10.1083/jcb.200605106
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发表时间：
2006-09-25
期刊：
影响因子：
--
通讯作者：
Schekman R
中科院分区：
文献类型：
--
作者：
Wang CW;Hamamoto S;Orci L;Schekman R
酵母细胞质膜蛋白Chs 3 p是从一个由高尔基体网络和内体系统组成的贮库转移到母芽颈的。两个TGN/内体外周蛋白，Chs 5 p和Chs 6p，和三个Chs 6p旁系同源物形成一个复合物，所需的TGN细胞表面运输的Chs 3 p。这些外周蛋白的作用尚不清楚，我们现在提供的证据表明，它们产生了一个外壳复合物，用于捕获膜蛋白到细胞表面。Sec 7 p是一种高尔基体蛋白，一般膜运输所需，并作为三磷酸鸟苷（GTP）结合蛋白Arf 1 p的核苷酸交换因子，需要在体内将Chs 5 p募集到TGN表面。在杆状病毒中表达的Chs 5 p、Chs 6p和Chs 6p旁系同源物的重组形式形成约1 MD的复合物，在需要酸性磷脂、Arf 1 p和不可水解GTPγS的反应中与合成脂质体结合。复合物保持与在蔗糖密度梯度上离心的脂质体结合。薄切片电子显微镜显示，与完整复合物Arf 1 p和GTPγS孵育的脂质体上存在尖刺状包衣结构。我们称之为新的外套外排体的作用，从TGN胞吐到细胞表面。不像其他外套（例如，外壳蛋白复合物I、II和网格蛋白/衔接蛋白复合物），外消旋体不在脂质体上形成芽或囊泡。
Ayeast plasma membrane protein, Chs3p, transits to the mother–bud neck from a reservoir comprising the trans-Golgi network (TGN) and endosomal system. Two TGN/endosomal peripheral proteins, Chs5p and Chs6p, and three Chs6p paralogues form a complex that is required for the TGN to cell surface transport of Chs3p. The role of these peripheral proteins has not been clear, and we now provide evidence that they create a coat complex required for the capture of membrane proteins en route to the cell surface. Sec7p, a Golgi protein required for general membrane traffic and functioning as a nucleotide exchange factor for the guanosine triphosphate (GTP)–binding protein Arf1p, is required to recruit Chs5p to the TGN surface in vivo. Recombinant forms of Chs5p, Chs6p, and the Chs6p paralogues expressed in baculovirus form a complex of approximately 1 MD that binds synthetic liposomes in a reaction requiring acidic phospholipids, Arf1p, and the nonhydrolyzable GTPγS. The complex remains bound to liposomes centrifuged on a sucrose density gradient. Thin section electron microscopy reveals a spiky coat structure on liposomes incubated with the full complex, Arf1p, and GTPγS. We termed the novel coat exomer for its role in exocytosis from the TGN to the cell surface. Unlike other coats (e.g., coat protein complex I, II, and clathrin/adaptor protein complex), the exomer does not form buds or vesicles on liposomes.
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影响因子：
2.9
作者：
Antonny, B;BeraudDufour, S;Chabre, M
通讯作者：
Chabre, M
影响因子：
7.7
作者：
Antonny, B;Gounon, P;Orci, L
通讯作者：
Orci, L
影响因子：
64.5
作者：
Kaksonen, M;Toret, CP;Drubin, DG
通讯作者：
Drubin, DG
影响因子：
64.5
作者：
NOVICK, P;FIELD, C;SCHEKMAN, R
通讯作者：
SCHEKMAN, R
影响因子：
64.5
作者：
Orci, L;Stamnes, M;Rothman, JE
通讯作者：
Rothman, JE