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驱动素连接蛋白内质网(ER)膜靶向信号的鉴定。

Identification of ER membrane targeting signal of kinectin.

作者信息

Abe Erika, Okawa Satoshi, Sugawara Masashiro, Watanabe Sumio, Toyoshima Itaru

机构信息

Department of Neurology, Akita University School of Medicine, 1-1-1 Hondo, Akita 010-8543, Japan.

出版信息

Neurosci Lett. 2007 Feb 21;413(3):238-40. doi: 10.1016/j.neulet.2006.11.064. Epub 2006 Dec 15.

Abstract

Kinectin has been identified as a kinesin receptor on endoplasmic reticulum (ER). The ER membrane binding domain of kinectin is still obscure and is thought to require a half of the molecule. To determine the ER insertion site, we produced several constructs around N-terminus of kinectin connected with green fluorescent protein (GFP) and visualized the distribution in Cos-7 cells. The fragment of residues 7-29 appeared in the reticular pattern exactly colocalized with the ER marker but did not remain for a long time. On the other hand, residues 1-106 maintained a reticular pattern for more than seven days. These results indicate that residues 7-29 of kinectin are sufficient for targeting to the ER membrane but insufficient for remaining on the ER.

摘要

驱动连接蛋白已被确定为内质网(ER)上的一种驱动蛋白受体。驱动连接蛋白的内质网膜结合结构域仍不清楚,并且被认为需要分子的一半。为了确定内质网插入位点,我们在驱动连接蛋白的N端周围构建了几个与绿色荧光蛋白(GFP)相连的构建体,并观察了其在Cos-7细胞中的分布。第7至29位残基的片段呈现出与内质网标记物完全共定位的网状模式,但不会长时间保留。另一方面,第1至106位残基保持网状模式超过7天。这些结果表明,驱动连接蛋白的第7至29位残基足以靶向内质网膜,但不足以在内质网上保留。

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