ArticleNature communications2024
ER-associated VAP27-1 and VAP27-3 proteins functionally link the lipid-binding ORP2A at the ER-chloroplast contact sites.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed.
- Lipid metabolism and contact site homologs are present at the chloroplast envelope-thylakoid interface.Nature communications · 2026Article
- Pyramiding elite alleles of the genetically linked OsNRAMP5 and OsHMA3 confers low Cd accumulation in rice grains without compromising stress tolerance.Plant communications · 2026Article
- Proximity Labelling-Based Proteomics Identifies Antiviral Host Factors Associated With the Potexvirus Replicase.Molecular plant pathology · 2026Article
- Plant plastids: from evolutionary origins to functional specialization and organelle interactions.Journal of experimental botany · 2025Review
- Key challenges and recommendations for defining organelle membrane contact sites.Nature reviews. Molecular cell biology · 2025Review
- Review
- The Extended Synaptotagmins ofPlants (Basel, Switzerland) · 2025Review
- The photosensitive endoplasmic reticulum-chloroplast contact site.Journal of microscopy · 2025Article
- Roles of non-specific lipid transfer proteins in plant defense: structural and functional perspectives.Frontiers in fungal biology · 2025Review
- Via Proteins and Lipids - Versatility of VAPs at Dynamic Membrane Contact Sites.Contact (Thousand Oaks (Ventura County, Calif.))Article
- Plant NETWORKED and VAP27 Proteins Work in Complexes to Regulate Membrane-Based Functions.Contact (Thousand Oaks (Ventura County, Calif.))Review
- Article
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Authors and funding
10 authors.
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Abstract
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.
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