Role of syntaxin 18 in the organization of endoplasmic reticulum subdomains

Role of syntaxin 18 in the organization of endoplasmic reticulum subdomains
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DOI:
10.1242/jcs.036103
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发表时间:
2009-05-15
影响因子:
4
通讯作者:
Tani, Katsuko
Tani, Katsuko
中科院分区:
生物学2区
文献类型:
--
作者:
Iinuma, Takayuki;Aoki, Takehiro;Tani, Katsuko

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内质网(ER)中亚结构域的存在使该细胞器能够执行各种功能,但其组织机制尚不清楚。在本研究中,我们发现syntaxin 18,一种定位于内质网的SNAP(可溶性NSF附着蛋白)受体,对于内质网两个亚结构域、光滑/粗糙内质网膜和内质网出口位点的组织是重要的。syntaxin 18的敲低引起内质网膜结构的全局变化,导致光滑内质网和粗糙内质网的分离。此外,随着ER-olgi中间区和高尔基复合体的分散,内质网出口位点的组织也发生了明显的变化。通过用brefeldin A(一种刺激逆行膜流向内质网的试剂)处理syntaxin-18缺失的细胞,内质网的这些形态学变化基本上恢复了。这些结果表明syntaxin 18通过介导逆行膜载体与内质网膜的融合在内质网亚域组织中起重要作用。
The presence of subdomains in the endoplasmic reticulum ( ER) enables this organelle to perform a variety of functions, yet the mechanisms underlying their organization are poorly understood. In the present study, we show that syntaxin 18, a SNAP (soluble NSF attachment protein) receptor localized in the ER, is important for the organization of two ER subdomains, smooth/rough ER membranes and ER exit sites. Knockdown of syntaxin 18 caused a global change in ER membrane architecture, leading to the segregation of the smooth and rough ER. Furthermore, the organization of ER exit sites was markedly changed concomitantly with dispersion of the ER-olgi intermediate compartment and the Golgi complex. These morphological changes in the ER were substantially recovered by treatment of syntaxin-18-depleted cells with brefeldin A, a reagent that stimulates retrograde membrane flow to the ER. These results suggest that syntaxin 18 has an important role in ER subdomain organization by mediating the fusion of retrograde membrane carriers with the ER membrane.