ArticleThe Plant cell2021
LDIP cooperates with SEIPIN and LDAP to facilitate lipid droplet biogenesis in Arabidopsis.
Article in The Plant cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 65 citations in OpenAlex.
- Single-Cell Transcriptomics Reveals the FA9-VAP Module Regulating Fatty Acid Accumulation in Soybean Seeds.Plant biotechnology journal · 2026Article
- Functional analysis of LIPID TRANSFER PROTEIN 6 (LTP6) in pennycress and Arabidopsis reveals divergent roles in oil storage and seed coat development.The Plant journal : for cell and molecular biology · 2026Article
- Lipid droplet proteome plasticity in plant evolution, growth and development, and response to stress.Journal of experimental botany · 2026Review
- BnaC03.SEIPIN1 improves seed oil content by increasing the number of lipid droplets in Brassica napus.BMC plant biology · 2026Article
- Lipid droplets at the interface of plant defense and pathogen exploitation.Frontiers in plant science · 2026Review
- Arabidopsis root lipid droplets are hubs for membrane homeostasis under heat stress, and triterpenoid synthesis and storage.The New phytologist · 2026Article
- Functional study of Phaeodactylum tricornutum Seipin highlights specificities of lipid droplets biogenesis in diatoms.The New phytologist · 2025Article
- Cell death-inducing DNA fragmentation factor alpha (DFFA)-like effectors (CIDEs) improve lipid droplet (LD) formation and oil accumulation in plant tissues.Plant biotechnology journal · 2025Article
- The jojoba lipid droplet protein LDAP1 facilitates the packaging of wax esters into lipid droplets.The Plant cell · 2025Article
- LIPID DROPLET PROTEIN OF SEEDS is involved in the control of lipid droplet size in Arabidopsis seeds and seedlings.The Plant cell · 2025Article
- Identification and Characterization of Lipid Droplet-Associated Protein (LDAP) Isoforms from Tung Tree (Plants (Basel, Switzerland) · 2025Article
- Inducible expression of DEFECTIVE IN ANTHER DEHISCENCE 1 enhances triacylglycerol accumulation and lipid droplet formation in vegetative tissues.The Plant journal : for cell and molecular biology · 2025Article
- Plasticity of the Arabidopsis leaf lipidome and proteome in response to pathogen infection and heat stress.Plant physiology · 2025Article
- Lipid droplets in plants: turnover and stress responses.Frontiers in plant science · 2025Review
- Transcriptomic and proteomic analysis of oil body associated protein dynamics in the biofuel feedstock Pennycress (Frontiers in plant science · 2025Article
- Exploiting lipid droplet metabolic pathway to foster lipid production: oleosin in focus.Plant cell reports · 2024Review
- α/β hydrolase domain-containing protein 1 acts as a lysolipid lipase and is involved in lipid droplet formation.National science review · 2024Article
- Targeted modulation of pennycress lipid droplet proteins impacts droplet morphology and seed oil content.The Plant journal : for cell and molecular biology · 2024Article
- Regulatory role ofHorticulture research · 2024Article
- A unifying mechanism for seipin-mediated lipid droplet formation.FEBS letters · 2024Review
Corrections and comments
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Authors and funding
19 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cytoplasmic lipid droplets (LDs) are evolutionarily conserved organelles that store neutral lipids and play critical roles in plant growth, development, and stress responses. However, the molecular mechanisms underlying their biogenesis at the endoplasmic reticulum (ER) remain obscure. Here we show that a recently identified protein termed LD-associated protein [LDAP]-interacting protein (LDIP) works together with both endoplasmic reticulum-localized SEIPIN and the LD-coat protein LDAP to facilitate LD formation in Arabidopsis thaliana. Heterologous expression in insect cells demonstrated that LDAP is required for the targeting of LDIP to the LD surface, and both proteins are required for the production of normal numbers and sizes of LDs in plant cells. LDIP also interacts with SEIPIN via a conserved hydrophobic helix in SEIPIN and LDIP functions together with SEIPIN to modulate LD numbers and sizes in plants. Further, the co-expression of both proteins is required to restore normal LD production in SEIPIN-deficient yeast cells. These data, combined with the analogous function of LDIP to a mammalian protein called LD Assembly Factor 1, are discussed in the context of a new model for LD biogenesis in plant cells with evolutionary connections to LD biogenesis in other eukaryotes.
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