COPII proteins exhibit distinct subdomains within each ER exit site for executing their functions
COPII proteins exhibit distinct subdomains within each ER exit site for executing their functions
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COPII 蛋白在每个 ER 出口位点内表现出不同的子域来执行其功能
DOI：
10.1038/s41598-019-43813-3
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发表时间：
2019
影响因子：
4.6
通讯作者：
Saito Kota
中科院分区：
文献类型：
--
作者：
Maeda Miharu;Kurokawa Kazuo;Katada Toshiaki;Nakano Akihiko;Saito Kota
分泌蛋白通过COPII包被的载体从内质网（ER）的特殊结构域（称为ER出口位点）输出。我们最近发现，TANGO 1和Sec 16合作组织哺乳动物ER出口网站的有效分泌。然而，哺乳动物内质网出口网站的详细空间组织尚未被揭示。在这里，我们使用超分辨率共聚焦实时成像显微镜（SCLIM）来研究内源性蛋白质的定位，并确定了与Sec 16并列的跨膜复合物（TANGO 1/cTAGE 5/Sec 12）中丰富的结构域。有趣的是，该结构域可以从每个哺乳动物ER出口位点内的COPII蛋白的内涂层和外涂层中区分出来。货物部分集中在分泌领域。我们的研究结果表明，哺乳动物ER出口网站区室化蛋白质根据其功能COPII囊泡的形成。
Secretory proteins are exported from special domains of the endoplasmic reticulum (ER) termed ER exit sites, via COPII-coated carriers. We recently showed that TANGO1 and Sec16 cooperatively organize mammalian ER exit sites for efficient secretion. However, the detailed spatial organization of mammalian ER exit sites is yet to be revealed. Here, we used super-resolution confocal live imaging microscopy (SCLIM) to investigate the localization of endogenous proteins, and we identified domains abundant in transmembrane complexes (TANGO1/cTAGE5/Sec12) juxtaposed to Sec16. Interestingly, this domain can be distinguished from the inner and the outer coats of COPII proteins within each mammalian ER exit site. Cargoes are partially concentrated in the domain for secretion. Our results suggest that mammalian ER exit sites compartmentalize proteins according to their function in COPII vesicle formation.