HIGH STEROL ESTER 1 is a key factor in plant sterol homeostasis.
Acyltransferases
/ metabolism
Arabidopsis
/ enzymology
Arabidopsis Proteins
/ genetics
Endoplasmic Reticulum
/ metabolism
Gene Expression Regulation, Enzymologic
Gene Expression Regulation, Plant
Genes, Plant
Homeostasis
Hydroxymethylglutaryl CoA Reductases
/ genetics
Membrane Proteins
/ genetics
Mutation
Phytosterols
/ metabolism
Plant Leaves
/ metabolism
Journal
Nature plants
ISSN: 2055-0278
Titre abrégé: Nat Plants
Pays: England
ID NLM: 101651677
Informations de publication
Date de publication:
11 2019
11 2019
Historique:
received:
27
12
2017
accepted:
18
09
2019
entrez:
13
11
2019
pubmed:
13
11
2019
medline:
9
4
2020
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 31712757
doi: 10.1038/s41477-019-0537-2
pii: 10.1038/s41477-019-0537-2
doi:
Substances chimiques
Arabidopsis Proteins
0
At1g60995 protein, Arabidopsis
0
Membrane Proteins
0
Phytosterols
0
Hydroxymethylglutaryl CoA Reductases
EC 1.1.1.-
Acyltransferases
EC 2.3.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1154-1166Commentaires et corrections
Type : CommentIn
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