A lipid viewpoint on the plant endoplasmic reticulum stress response

被引:13
作者
Kanehara, Kazue [1 ]
Cho, Yueh [1 ]
Yu, Chao-Yuan [1 ]
机构
[1] Acad Sinica, Inst Plant & Microbial Biol, Taipei 11529, Taiwan
关键词
Arabidopsis thaliana; endoplasmic reticulum stress; fatty acid; inositol; INOSITOL-REQUIRING ENZYME1; lipid; membrane saturation; phospholipids; unfolded protein response; UNFOLDED PROTEIN RESPONSE; RECEPTOR-LIKE KINASES; TRANSCRIPTION FACTOR; ARABIDOPSIS DEFICIENT; PHOSPHATIDYLCHOLINE BIOSYNTHESIS; PHOSPHOLIPID UNSATURATION; GENETIC-CHARACTERIZATION; INOSITOL PYROPHOSPHATES; TRANSMEMBRANE PROTEIN; SIGNAL-TRANSDUCTION;
D O I
10.1093/jxb/erac063
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
This review discusses the plant unfolded protein response from the perspective of membrane phospholipids in comparison with the respective systems in other model organisms. Organisms, including humans, seem to be constantly exposed to various changes, which often have undesirable effects, referred to as stress. To keep up with these changes, eukaryotic cells may have evolved a number of relevant cellular processes, such as the endoplasmic reticulum (ER) stress response. Owing to presumably intimate links between human diseases and the ER function, the ER stress response has been extensively investigated in various organisms for a few decades. Based on these studies, we now have a picture of the molecular mechanisms of the ER stress response, one of which, the unfolded protein response (UPR), is highly conserved among yeasts, mammals, higher plants, and green algae. In this review, we attempt to highlight the plant UPR from the perspective of lipids, especially membrane phospholipids. Phosphatidylcholine (PtdCho) and phosphatidylethanolamine (PtdEtn) are the most abundant membrane phospholipids in eukaryotic cells. The ratio of PtdCho to PtdEtn and the unsaturation of fatty acyl tails in both phospholipids may be critical factors for the UPR, but the pathways responsible for PtdCho and PtdEtn biosynthesis are distinct in animals and plants. We discuss the plant UPR in comparison with the system in yeasts and animals in the context of membrane phospholipids.
引用
收藏
页码:2835 / 2847
页数:13
相关论文
共 114 条
[61]   Degradation of the Endoplasmic Reticulum by Autophagy during Endoplasmic Reticulum Stress in Arabidopsis [J].
Liu, Yimo ;
Burgos, Junmarie Soto ;
Deng, Yan ;
Srivastava, Renu ;
Howell, Stephen H. ;
Bassham, Diane C. .
PLANT CELL, 2012, 24 (11) :4635-4651
[62]   Role of Aminoalcoholphosphotransferases 1 and 2 in Phospholipid Homeostasis in Arabidopsis [J].
Liu, Yu ;
Wang, Geliang ;
Wang, Xuemin .
PLANT CELL, 2015, 27 (05) :1512-1528
[63]   A Methyltransferase Trio Essential for Phosphatidylcholine Biosynthesis and Growth [J].
Liu, Yu-chi ;
Lin, Ying-Chen ;
Kanehara, Kazue ;
Nakamura, Yuki .
PLANT PHYSIOLOGY, 2019, 179 (02) :433-445
[64]   Phospholipid metabolism regulated by a transcription factor sensing phosphatidic acid [J].
Loewen, CJR ;
Gaspar, ML ;
Jesch, SA ;
Delon, C ;
Ktistakis, NT ;
Henry, SA ;
Levine, TP .
SCIENCE, 2004, 304 (5677) :1644-1647
[65]   A MUTATION AT THE FAD8 LOCUS OF ARABIDOPSIS IDENTIFIES A 2ND CHLOROPLAST OMEGA-3 DESATURASE [J].
MCCONN, M ;
HUGLY, S ;
BROWSE, J ;
SOMERVILLE, C .
PLANT PHYSIOLOGY, 1994, 106 (04) :1609-1614
[66]   A sub-proteome of Arabidopsis thaliana mature stems trapped on Concanavalin A is enriched in cell wall glycoside hydrolases [J].
Minic, Zoran ;
Jamet, Elisabeth ;
Negroni, Luc ;
der Garabedian, P. Arsene ;
Zivy, Michel ;
Jouanin, Lise .
JOURNAL OF EXPERIMENTAL BOTANY, 2007, 58 (10) :2503-2512
[67]  
MIQUEL M, 1992, J BIOL CHEM, V267, P1502
[68]   Defects in IRE1 enhance cell death and fail to degrade mRNAs encoding secretory pathway proteins in the Arabidopsis unfolded protein response [J].
Mishiba, Kei-ichiro ;
Nagashima, Yukihiro ;
Suzuki, Eiji ;
Hayashi, Noriko ;
Ogata, Yoshiyuki ;
Shimada, Yukihisa ;
Koizumi, Nozomu .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2013, 110 (14) :5713-5718
[69]   Defects in CTP: PHOSPHORYLETHANOLAMINE CYTIDYLYLTRANSFERASE affect embryonic and postembryonic development in Arabidopsis [J].
Mizoi, Junya ;
Nakamura, Masanobu ;
Nishida, Ikuo .
PLANT CELL, 2006, 18 (12) :3370-3385
[70]   Inositol phospholipid metabolism in Arabidopsis. Characterized and putative isoforms of inositol phospholipid kinase and phosphoinositide-specific phospholipase C [J].
Mueller-Roeber, B ;
Pical, C .
PLANT PHYSIOLOGY, 2002, 130 (01) :22-46