The Golgi-Localized Arabidopsis Endomembrane Protein12 Contains Both Endoplasmic Reticulum Export and Golgi Retention Signals at Its C Terminus

Endomembrane proteins (EMPs), belonging to the evolutionarily conserved transmembrane nine superfamily in yeast and mammalian cells, are characterized by the presence of a large lumenal N terminus, nine transmembrane domains, and a short cytoplasmic tail. The Arabidopsis thaliana genome contains 12...

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Published inThe Plant cell Vol. 24; no. 5; pp. 2086 - 2104
Main Authors Gao, Caiji, Yu, Christine K. Y., Qu, Song, San, Melody Wan Yan, Li, Kwun Yee, Lo, Sze Wan, Jiang, Liwen
Format Journal Article
LanguageEnglish
Published United States American Society of Plant Biologists 01.05.2012
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Summary:Endomembrane proteins (EMPs), belonging to the evolutionarily conserved transmembrane nine superfamily in yeast and mammalian cells, are characterized by the presence of a large lumenal N terminus, nine transmembrane domains, and a short cytoplasmic tail. The Arabidopsis thaliana genome contains 12 EMP members [EMP1 to EMP12), but little is known about their protein subcellular localization and function. Here, we studied the subcellular localization and targeting mechanism of EMP12 in Arabidopsis and demonstrated that (1) both endogenous EMP12 (detected by EMP12 antibodies) and green fluorescent protein (GFP)-EMPI 2 fusion localized to the Golgi apparatus in transgenic Arabidopsis plants; (2) GFP fusion at the terminus of EMP12 caused mislocalization of EMP12-GFP to reach post-Golgi compartments and vacuoles for degradation in Arabidopsis cells; (3) the EMP12 cytoplasmic tail contained dual sorting signals (i. e., an endoplasmic reticulum export motif and a Golgi retention signal that interacted with COPII and COPI subunits, respectively); and (4) the Golgi retention motif of EMP12 retained several post-Golgi membrane proteins within the Golgi apparatus in gain-of-function analysis. These sorting signals are highly conserved in all plant EMP isoforms and, thus, likely represent a general mechanism for EMP targeting in plant cells.
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Some figures in this article are displayed in color online but in black and white in the print edition.
www.plantcell.org/cgi/doi/10.1105/tpc.112.096057
Online version contains Web-only data.
The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantcell.org) is: Liwen Jiang (ljiang@cuhk.edu.hk).
ISSN:1040-4651
1532-298X
DOI:10.1105/tpc.112.096057