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Arabidopsis ENDOMEMBRANE PROTEIN 12 contributes to the endoplasmic reticulum stress response by regulating K/HDEL receptor trafficking

King Pong Leung, Ming Luo, Caiji Gao, Yonglun Zeng, Qiong Zhao, Mee-Len Chye, Xiaoqiang Yao, Liwen Jiang
King Pong Leung
The Chinese University of Hong Kong CITY: Hong Kong Hong Kong [HK]
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  • For correspondence: kpsleung1990@gmail.com
Ming Luo
South China Botanical Garden, Chinese Academy of Sciences CITY: Guangzhou POSTAL_CODE: 510650 China [CN]
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  • For correspondence: luoming@scbg.ac.cn
Caiji Gao
South China Normal University CITY: GUANGZHOU STATE: Guangdong Province POSTAL_CODE: 510631 China [CN]
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  • For correspondence: gaocaiji@m.scnu.edu.cn
Yonglun Zeng
The Chinese University of Hong Kong CITY: Hong Kong Hong Kong [HK]
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  • For correspondence: zengyonglun.allen@gmail.com
Qiong Zhao
The Chinese University of Hong Kong CITY: Hong Kong China [CN]
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  • For correspondence: arabidopsis007@gmail.com
Mee-Len Chye
The University of Hong Kong CITY: Hong Kong China [CN]
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  • For correspondence: mlchye@hku.hk
Xiaoqiang Yao
The Chinese University of Hong Kong CITY: Hong Kong China [CN]
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  • For correspondence: yao2068@cuhk.edu.hk
Liwen Jiang
The Chinese University of Hong Kong CITY: Hong Kong China [CN]
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  • For correspondence: ljiang@cuhk.edu.hk

Published June 2019. DOI: https://doi.org/10.1105/tpc.18.00913

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  • © 2019 American Society of Plant Biologists. All rights reserved.

Abstract

ENDOMEMBRANE PROTEIN 70 (EMP70) proteins constitute a 12-member superfamily in Arabidopsis thaliana, and are the most abundant protein species in plant Golgi proteomes. However, the physiological functions of EMPs in plants remain largely unknown. Here we have demonstrated that two AtEMP12 T-DNA insertion mutants are sensitive to ER (endoplasmic reticulum) stress as induced by tunicamycin and dithiothreitol treatments. Interestingly, the unfolded protein response (UPR) is constitutively activated in the knockout mutant emp12-1 under normal growth conditions, suggesting that the activation is a result of insufficient chaperones in the ER to aid protein folding. Indeed, we have further shown that BiP is secreted into the apoplast in emp12-1, while the K/HDEL receptor ERD2a, which regulates BiP trafficking, is exclusively localized in the ER in emp12-1, instead of its known ER-Golgi dual-localization. Given an enhanced retrograde transport of ERD2a, along with less dimerized receptor formed in the absence of EMP12, ERD2a may be prematurely returned to the ER without its bound ligands. Therefore, we propose that EMP12 may act as a novel regulator of the K/HDEL receptor to ensure an effective retrograde transport of K/HDEL ligands.

  • Received December 3, 2018.
  • Accepted May 15, 2019.
  • Published May 23, 2019.
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EMP12 maintains Golgi localization of ERD2a
King Pong Leung, Ming Luo, Caiji Gao, Yonglun Zeng, Qiong Zhao, Mee-Len Chye, Xiaoqiang Yao, Liwen Jiang
The Plant Cell Jun 2019, tpc.00913.2018; DOI: 10.1105/tpc.18.00913

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EMP12 maintains Golgi localization of ERD2a
King Pong Leung, Ming Luo, Caiji Gao, Yonglun Zeng, Qiong Zhao, Mee-Len Chye, Xiaoqiang Yao, Liwen Jiang
The Plant Cell Jun 2019, tpc.00913.2018; DOI: 10.1105/tpc.18.00913
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The Plant Cell: 32 (12)
The Plant Cell
Vol. 32, Issue 12
Dec 2020
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