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Title: HIGH STEROL ESTER 1 is a key factor in plant sterol homeostasis
Authors: Shimada, Takashi L.
Shimada, Tomoo
Okazaki, Yozo
Higashi, Yasuhiro
Saito, Kazuki
Kuwata, Keiko
Oyama, Kaori
Kato, Misako
Ueda, Haruko
Nakano, Akihiko
Ueda, Takashi
Takano, Yoshitaka  kyouindb  KAKEN_id  orcid (unconfirmed)
Hara-Nishimura, Ikuko
Author's alias: 島田, 貴士
嶋田, 知生
岡咲, 洋三
東, 弘
斉藤, 和季
桑田, 啓子
小山, 香梨
加藤, 美砂子
上田, 晴子
中野, 明彦
上田, 貴志
高野, 義孝
西村, いくこ
Issue Date: Nov-2019
Publisher: Springer Science and Business Media LLC
Journal title: Nature Plants
Volume: 5
Issue: 11
Start page: 1154
End page: 1166
Abstract: Plants strictly regulate the levels of sterol in their cells, as high sterol levels are toxic. However, how plants achieve sterol homeostasis is not fully understood. We isolated an Arabidopsis thaliana mutant that abundantly accumulated sterol esters in structures of about 1 µm in diameter in leaf cells. We designated the mutant high sterol ester 1 (hise1) and called the structures sterol ester bodies. Here, we show that HISE1, the gene product that is altered in this mutant, functions as a key factor in plant sterol homeostasis on the endoplasmic reticulum (ER) and participates in a fail-safe regulatory system comprising two processes. First, HISE1 downregulates the protein levels of the β-hydroxy β-methylglutaryl-CoA reductases HMGR1 and HMGR2, which are rate-limiting enzymes in the sterol synthesis pathway, resulting in suppression of sterol overproduction. Second, if the first process is not successful, excess sterols are converted to sterol esters by phospholipid sterol acyltransferase1 (PSAT1) on ER microdomains and then segregated in SE bodies.
Description: ステロールの過剰集積を防ぐ植物の技を解明 --二段階フェイルセーフ・システム--. 京都大学プレスリリース. 2019-11-15.
Rights: This is the accepted manuscript of the article, which has been published in final form at
The full-text file will be made open to the public on 11 May 2020 in accordance with publisher's 'Terms and Conditions for Self-Archiving'.
This is not the published version. Please cite only the published version.
DOI(Published Version): 10.1038/s41477-019-0537-2
PubMed ID: 31712757
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