ArticleJournal of cell science2012
ER-shaping proteins facilitate lipid exchange between the ER and mitochondria in S. cerevisiae.
Article in Journal of cell science, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
54 citing papers in PubMed, 111 citations in OpenAlex.
- Mitochondrial membrane remodeling in stress adaptation: Lipid control of organelle quality.Protein science : a publication of the Protein Society · 2026Review
- Mitochondrial interplay with membrane organelles in health and disease.Cell communication and signaling : CCS · 2026Review
- A dual-purification system to isolate mitochondrial subpopulations.Journal of cell science · 2025Article
- Review
- Organelle activity organized by the endoplasmic reticulum-mitochondria encounter structure -ERMES- is essential forMicrobial cell (Graz, Austria) · 2025Article
- Imaging and proteomics toolkits for studying organelle contact sites.Frontiers in cell and developmental biology · 2024Review
- PERK recruits E-Syt1 at ER-mitochondria contacts for mitochondrial lipid transport and respiration.The Journal of cell biology · 2023Article
- Molecular species selectivity of lipid transport creates a mitochondrial sink for di-unsaturated phospholipids.The EMBO journal · 2022Article
- Mitochondria-endoplasmic reticulum contacts in sepsis-induced myocardial dysfunction.Frontiers in cell and developmental biology · 2022Review
- Mechanisms of nonvesicular lipid transport.The Journal of cell biology · 2021Review
- One ring to bring them all and in the darkness bind them: The trafficking of heme without deliverers.Biochimica et biophysica acta. Molecular cell research · 2021Review
- 3D Dissection of Structural Membrane-Wall Contacts in Filamentous Moss Protonemata.International journal of molecular sciences · 2020Article
- High-Throughput Identification of Nuclear Envelope Protein Interactions inG3 (Bethesda, Md.) · 2020Article
- Phospholipid ebb and flow makes mitochondria go.The Journal of cell biology · 2020Review
- Miga-mediated endoplasmic reticulum-mitochondria contact sites regulate neuronal homeostasis.eLife · 2020Article
- The Molecular Determinants of Mitochondrial Membrane Contact With ER, Lysosomes and Peroxisomes in Neuronal Physiology and Pathology.Frontiers in cellular neuroscience · 2020Article
- Tricalbin-Mediated Contact Sites Control ER Curvature to Maintain Plasma Membrane Integrity.Developmental cell · 2019Article
- Tricalbins Contribute to Cellular Lipid Flux and Form Curved ER-PM Contacts that Are Bridged by Rod-Shaped Structures.Developmental cell · 2019Article
- Article
- Phospholipid transport protein function at organelle contact sites.Current opinion in cell biology · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The endoplasmic reticulum (ER) forms a network of sheets and tubules that extends throughout the cell. Proteins required to maintain this complex structure include the reticulons, reticulon-like proteins, and dynamin-like GTPases called atlastins in mammals and Sey1p in Saccharomyces cerevisiae. Yeast cells missing these proteins have abnormal ER structure, particularly defects in the formation of ER tubules, but grow about as well as wild-type cells. We screened for mutations that cause cells that have defects in maintaining ER tubules to grow poorly. Among the genes we found were members of the ER mitochondria encounter structure (ERMES) complex that tethers the ER and mitochondria. Close contacts between the ER and mitochondria are thought to be sites where lipids are moved from the ER to mitochondria, a process that is required for mitochondrial membrane biogenesis. We show that ER to mitochondria phospholipid transfer slows significantly in cells missing both ER-shaping proteins and the ERMES complex. These cells also have altered steady-state levels of phospholipids. We found that the defect in ER to mitochondria phospholipid transfer in a strain missing ER-shaping proteins and a component of the ERMES complex was corrected by expression of a protein that artificially tethers the ER and mitochondria. Our findings indicate that ER-shaping proteins play a role in maintaining functional contacts between the ER and mitochondria and suggest that the shape of the ER at ER-mitochondria contact sites affects lipid exchange between these organelles.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.