ER-associated VAP27-1 and VAP27-3 proteins functionally link the lipid-binding ORP2A at the ER-chloroplast contact sites.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
17 Jul 2024
17 Jul 2024
Historique:
received:
01
12
2022
accepted:
09
07
2024
medline:
18
7
2024
pubmed:
18
7
2024
entrez:
17
7
2024
Statut:
epublish
Résumé
The plant endoplasmic reticulum (ER) contacts heterotypic membranes at membrane contact sites (MCSs) through largely undefined mechanisms. For instance, despite the well-established and essential role of the plant ER-chloroplast interactions for lipid biosynthesis, and the reported existence of physical contacts between these organelles, almost nothing is known about the ER-chloroplast MCS identity. Here we show that the Arabidopsis ER membrane-associated VAP27 proteins and the lipid-binding protein ORP2A define a functional complex at the ER-chloroplast MCSs. Specifically, through in vivo and in vitro association assays, we found that VAP27 proteins interact with the outer envelope membrane (OEM) of chloroplasts, where they bind to ORP2A. Through lipidomic analyses, we established that VAP27 proteins and ORP2A directly interact with the chloroplast OEM monogalactosyldiacylglycerol (MGDG), and we demonstrated that the loss of the VAP27-ORP2A complex is accompanied by subtle changes in the acyl composition of MGDG and PG. We also found that ORP2A interacts with phytosterols and established that the loss of the VAP27-ORP2A complex alters sterol levels in chloroplasts. We propose that, by interacting directly with OEM lipids, the VAP27-ORP2A complex defines plant-unique MCSs that bridge ER and chloroplasts and are involved in chloroplast lipid homeostasis.
Identifiants
pubmed: 39019917
doi: 10.1038/s41467-024-50425-7
pii: 10.1038/s41467-024-50425-7
doi:
Substances chimiques
Arabidopsis Proteins
0
monogalactosyldiacylglycerol
0
Galactolipids
0
Membrane Proteins
0
Receptors, Steroid
0
oxysterol binding protein
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
6008Subventions
Organisme : DOE | SC | Chemical Sciences, Geosciences, and Biosciences Division (Chemical Sciences, Geosciences, and Energy Biosciences)
ID : DE-FG02-91ER20021
Organisme : AgBioResearch, Michigan State University (MSU AgBioResearch)
ID : MICL02598
Informations de copyright
© 2024. The Author(s).
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