ArticleMolecular biology of the cell2021
Multiple C2 domain-containing transmembrane proteins promote lipid droplet biogenesis and growth at specialized endoplasmic reticulum subdomains.
Article in Molecular biology of the cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers, 1 of them a synthesis that pooled it.
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Who cites it
26 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Inter-organellar Communication in Parkinson's and Alzheimer's Disease: Looking Beyond Endoplasmic Reticulum-Mitochondria Contact Sites.Frontiers in neuroscience · 2022Pooled it
- Heterogeneity, dynamics and organelle interactions of lipid droplets.Nature reviews. Molecular cell biology · 2026Review
- In situ architecture of plasmodesmata in Physcomitrium patens resolved by cryo-electron tomography.Nature plants · 2026Article
- MCTP1 and MCTP2 promote ER-PM contact sites and regulate PI4P homeostasis and cell migration.Molecular biology of the cell · 2026Article
- The reticulon homology domain of Pex30 generates membrane curvature at ER subdomains for lipid droplet biogenesis.bioRxiv : the preprint server for biology · 2026Article
- Nvj3 regulates Dga1-mediated triacylglycerol synthesis and lipid droplet formation at ER contact sites.bioRxiv : the preprint server for biology · 2026Article
- DNA methylation predicts lung function and pulmonary exacerbation in sputum samples from patients with cystic fibrosis.Clinical epigenetics · 2025Article
- Navigating lipid droplet proteins - part I: ER targeting routes of lipid droplet-destined membrane proteins.Biochemical Society transactions · 2025Review
- Phosphatidic acid drives spatiotemporal distribution of Pex30 at ER-LD contact sites.The Journal of cell biology · 2025Article
- Spatial proteomics of ER tubules reveals CLMN, an ER-actin tether at focal adhesions that promotes cell migration.Cell reports · 2025Article
- New functions of B9D2 in tight junctions and epithelial polarity.Scientific reports · 2024Article
- A unifying mechanism for seipin-mediated lipid droplet formation.FEBS letters · 2024Review
- Lipid droplets and cellular lipid flux.Nature cell biology · 2024Review
- The evolving landscape of ER-LD contact sites.Frontiers in cell and developmental biology · 2024Review
- Concept of lipid droplet biogenesis.European journal of cell biology · 2023Review
- Early steps in the birth of four membrane-bound organelles-Peroxisomes, lipid droplets, lipoproteins, and autophagosomes.Current opinion in cell biology · 2023Review
- Lipid droplet biogenesis and functions in health and disease.Nature reviews. Endocrinology · 2023Review
- Glycerolipid Synthesis and Lipid Droplet Formation in the Endoplasmic Reticulum.Cold Spring Harbor perspectives in biology · 2023Review
- Cholesterol esters form supercooled lipid droplets whose nucleation is facilitated by triacylglycerols.Nature communications · 2023Article
- Skeletal Muscles of Sedentary and Physically Active Aged People Have Distinctive Genic Extrachromosomal Circular DNA Profiles.International journal of molecular sciences · 2023Article
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Authors and funding
4 authors.
Funding
Abstract
Lipid droplets (LDs) are neutral lipid-containing organelles enclosed in a single monolayer of phospholipids. LD formation begins with the accumulation of neutral lipids within the bilayer of the endoplasmic reticulum (ER) membrane. It is not known how the sites of formation of nascent LDs in the ER membrane are determined. Here we show that multiple C2 domain-containing transmembrane proteins, MCTP1 and MCTP2, are at sites of LD formation in specialized ER subdomains. We show that the transmembrane domain (TMD) of these proteins is similar to a reticulon homology domain. Like reticulons, these proteins tubulate the ER membrane and favor highly curved regions of the ER. Our data indicate that the MCTP TMDs promote LD biogenesis, increasing LD number. MCTPs colocalize with seipin, a protein involved in LD biogenesis, but form more stable microdomains in the ER. The MCTP C2 domains bind charged lipids and regulate LD size, likely by mediating ER-LD contact sites. Together, our data indicate that MCTPs form microdomains within ER tubules that regulate LD biogenesis, size, and ER-LD contacts. Interestingly, MCTP punctae colocalized with other organelles as well, suggesting that these proteins may play a general role in linking tubular ER to organelle contact sites.
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