cTAGE5 mediates collagen secretion through interaction with TANGO1 at endoplasmic reticulum exit sites.
cTAGE5 mediates collagen secretion through interaction with TANGO1 at endoplasmic reticulum exit sites.
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DOI：
10.1091/mbc.e11-02-0143
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发表时间：
2011-07-01
影响因子：
3.3
通讯作者：
Katada T
中科院分区：
文献类型：
--
作者：
Saito K;Yamashiro K;Ichikawa Y;Erlmann P;Kontani K;Malhotra V;Katada T
胶原蛋白的分泌机制尚不完全清楚。研究发现，cTAGE5与TANGO1结合，推测内质网输出的VII型胶原是由cTAGE5/TANGO1复合体驱动的。皮肤T细胞淋巴瘤相关抗原5(CTAGE5)是最早发现的一种肿瘤抗原，在多种肿瘤细胞系中呈高表达。该基因编码一个完整的膜蛋白，含有两个卷曲的基序和一个富含脯氨酸的结构域。我们发现cTAGE5特异性地定位于内质网(ER)退出部位。此外，cTAGE5通过其盘绕螺旋基序的相互作用，与先前鉴定的VII型胶原的货运受体TANGO1(MIA3)形成复合体。值得注意的是，cTAGE5和TANGO1能够通过其C末端的富含脯氨酸的结构域与COPII Sec23/24复合体的内层辅基相互作用，这是分泌VII型胶原所必需的。我们认为cTAGE5可能是内质网输出VII型胶原的共同受体。
The mechanism of collagen secretion is not completely understood. It is found that cTAGE5 binds to TANGO1, and it is suggested that collagen VII export from the ER is driven by a cTAGE5/TANGO1 complex. Cutaneous T-cell lymphoma-–associated antigen 5 (cTAGE5), an originally identified tumor antigen, is overexpressed in various cancer cell lines. The cDNA encodes an integral membrane protein containing two coiled-coil motifs and a proline-rich domain. We show that cTAGE5 specifically localizes to the endoplasmic reticulum (ER) exit sites. In addition, cTAGE5 forms a complex with TANGO1 (MIA3), a previously characterized cargo receptor for collagen VII, by the interaction of their coiled-coil motifs. Of interest, cTAGE5, as well as TANGO1, is capable of interacting with the inner-layer coatomer of COPII Sec23/24 complex through their C-terminal proline-rich domains and required for collagen VII secretion. We propose that cTAGE5 acts as a coreceptor of TANGO1 for collagen VII export from the ER.