Arl6IP1 has the ability to shape the mammalian ER membrane in a reticulon-like fashion.

Arl6IP1 has the ability to shape the mammalian ER membrane in a reticulon-like fashion.
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DOI:
10.1042/bj20131186
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发表时间:
2014-02
期刊:
The Biochemical journal
影响因子:
--
通讯作者:
Yasunori Yamamoto;Asuka Yoshida;N. Miyazaki;K. Iwasaki;T. Sakisaka
Yasunori Yamamoto;Asuka Yoshida;N. Miyazaki;K. Iwasaki;T. Sakisaka
中科院分区:
其他
文献类型:
--
作者:
Yasunori Yamamoto;Asuka Yoshida;N. Miyazaki;K. Iwasaki;T. Sakisaka

文献摘要

相似文献

内质网由核膜和由膜片和小管组成的外周网络组成。进化上保守的两类ER膜蛋白,网状和Reep(受体表达增强蛋白)/DP1(在息肉病基因1中缺失)/Yop1(Yip 1伴侣)形成了高曲率的ER小管。在哺乳动物中,到目前为止已经确定了四个网状蛋白家族成员和六个REEP家族成员。在本文中,我们报道了Arl6IP1(ADP-核糖化因子样6相互作用蛋白1),它是一种多细胞生物特有的抗凋亡蛋白,在哺乳动物细胞的内质网小管的形成中具有潜在的作用。Arl6IP1与网状蛋白的初级序列同源性不高,它含有网状短发夹状跨膜结构域,并与介导管状ER网络形成的GTP酶atlastin结合。Arl6IP1的过表达诱导了内质网广泛的管状结构,并排除了管腔蛋白。此外,Ar16IP1的过表达稳定了内质网小管,使细胞即使在没有微管的情况下也能保持内质网小管。Arl6IP1将脂质体压缩成小管。Ar16IP1的成膜活性需要跨膜区的短发夹状结构。本研究的结果表明,Arl6IP1具有以网状方式形成高曲率ER小管的能力。
The ER (endoplasmic reticulum) consists of the nuclear envelope and a peripheral network of membrane sheets and tubules. Two classes of the evolutionarily conserved ER membrane proteins, reticulons and REEPs (receptor expression-enhancing proteins)/DP1 (deleted in polyposis locus 1)/Yop1 (YIP 1 partner), shape high-curvature ER tubules. In mammals, four members of the reticulon family and six members of the REEP family have been identified so far. In the present paper we report that Arl6IP1(ADP-ribosylation factor-like 6 interacting protein 1), an anti-apoptotic protein specific to multicellular organisms, is a potential player in shaping the ER tubules in mammalian cells. Arl6IP1, which does not share an overall primary sequence homology with reticulons, harbours reticulon-like short hairpin transmembrane domains and binds to atlastin, a GTPase that mediates the formation of the tubular ER network. Overexpression of Arl6IP1 induced extensive tubular structures of the ER and excluded a luminal protein. Furthermore, overexpression of Arl6IP1 stabilized the ER tubules, allowing the cells to maintain the ER tubules even in the absence of microtubules. Arl6IP1 constricted liposomes into tubules. The short hairpin structures of the transmembrane domains were required for the membrane-shaping activity of Arl6IP1. The results of the present study indicate that Arl6IP1 has the ability to shape high-curvature ER tubules in a reticulon-like fashion.