Two hydrophobic segments of the RTN1 family determine the ER localization and retention

被引：12

作者：

Iwahashi, Jun ^{[1
]}

Hamada, Nobuyuki ^{[1
]}

Watanabe, Hiroshi ^{[1
]}

机构：

[1] Kurume Univ, Sch Med, Dept Infect Med, Div Infect Dis, Kurume, Fukuoka 8300011, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2007年 / 355卷 / 02期

关键词：

reticulon; RTN1-A; localization; endoplasmic reticulum; ER retention;

D O I：

10.1016/j.bbrc.2007.02.001

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

apoptosis, inhibiting axonal regeneration, and Alzheimer's disease. The RTN proteins are produced without an N-terminal signal peptide. Their C-terminal domain contains two long hydrophobic segments. We analyzed the ER localization signal of human RTN1-A. Mutant proteins lacking the first (39 residues) or second (36 residues) hydrophobic segment showed ER localization. On the other hand, the mutant lacking both hydrophobic segments was cytosolic. Enhanced green fluorescent protein (EGFP) tagged with the first or second hydrophobic segment of RTN1-A was localized to the ER. These results suggest that each hydrophobic segment determines the ER localization. In addition, EGFP tagged with the truncated form of the first hydrophobic segment exhibited the localization to the Golgi rather than the ER. This suggests that the length of the hydrophobic segment contributes to the ER retention of RTN1-A. (c) 2007 Elsevier Inc. All rights reserved.

引用

页码：508 / 512

页数：5

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