ArticleEMBO reports2015
Structural basis of intramitochondrial phosphatidic acid transport mediated by Ups1-Mdm35 complex.
Article in EMBO reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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.
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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
30 citing papers in PubMed, 61 citations in OpenAlex.
- Ubiquitination regulation of mitochondrial homeostasis: a new sight for the treatment of gastrointestinal tumors.Frontiers in immunology · 2025Review
- The UbiB family member Cqd1 forms a novel membrane contact site in mitochondria.Journal of cell science · 2023Article
- Arabidopsis Sec14 proteins (SFH5 and SFH7) mediate interorganelle transport of phosphatidic acid and regulate chloroplast development.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Role of SEC14-like phosphatidylinositol transfer proteins in membrane identity and dynamics.Frontiers in plant science · 2023Review
- Quantitative Models of Lipid Transfer and Membrane Contact Formation.Contact (Thousand Oaks (Ventura County, Calif.)) · 2022Article
- Relevance of the TRIAP1/p53 axis in colon cancer cell proliferation and adaptation to glutamine deprivation.Frontiers in oncology · 2022Article
- Mechanisms of Non-Vesicular Exchange of Lipids at Membrane Contact Sites: Of Shuttles, Tunnels and, Funnels.Frontiers in cell and developmental biology · 2021Review
- New Era of Diacylglycerol Kinase, Phosphatidic Acid and Phosphatidic Acid-Binding Protein.International journal of molecular sciences · 2020Review
- Molecular mechanism of mitochondrial phosphatidate transfer by Ups1.Communications biology · 2020Article
- Phospholipid ebb and flow makes mitochondria go.The Journal of cell biology · 2020Review
- Article
- Lipid metabolism-related proteins of relevant evolutionary and lymphoid interest (PRELI) domain containing family proteins in cancer.American journal of translational research · 2020Review
- Proteolytic Control of Lipid Metabolism.ACS chemical biology · 2019Review
- Mitochondrial protein-induced stress triggers a global adaptive transcriptional programme.Nature cell biology · 2019Article
- Structural determinants of lipid specificity within Ups/PRELI lipid transfer proteins.Nature communications · 2019Article
- An Isoprene Lipid-Binding Protein Promotes Eukaryotic Coenzyme Q Biosynthesis.Molecular cell · 2019Article
- Lipid transfer proteins: the lipid commute via shuttles, bridges and tubes.Nature reviews. Molecular cell biology · 2019Review
- Maintenance of Cardiolipin and Crista Structure Requires Cooperative Functions of Mitochondrial Dynamics and Phospholipid Transport.Cell reports · 2019Article
- Lipid transfer proteins rectify inter-organelle flux and accurately deliver lipids at membrane contact sites.Journal of lipid research · 2018Review
- Cooperative function of Fmp30, Mdm31, and Mdm32 in Ups1-independent cardiolipin accumulation in the yeast Saccharomyces cerevisiae.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ups1 forms a complex with Mdm35 and is critical for the transport of phosphatidic acid (PA) from the mitochondrial outer membrane to the inner membrane. We report the crystal structure of the Ups1-Mdm35-PA complex and the functional characterization of Ups1-Mdm35 in PA binding and transfer. Ups1 features a barrel-like structure consisting of an antiparallel β-sheet and three α-helices. Mdm35 adopts a three-helical clamp-like structure to wrap around Ups1 to form a stable complex. The β-sheet and α-helices of Ups1 form a long tunnel-like pocket to accommodate the substrate PA, and a short helix α2 acts as a lid to cover the pocket. The hydrophobic residues lining the pocket and helix α2 are critical for PA binding and transfer. In addition, a hydrophilic patch on the surface of Ups1 near the PA phosphate-binding site also plays an important role in the function of Ups1-Mdm35. Our study reveals the molecular basis of the function of Ups1-Mdm35 and sheds new light on the mechanism of intramitochondrial phospholipid transport by the MSF1/PRELI family proteins.
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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.