The DOI matches its Crossref record; 58 of the 58 references it cites were found in a registry or an index.
Structure–function insights into direct lipid transfer between membranes by Mmm1–Mdm12 of ERMES
Open accessAbstract
The endoplasmic reticulum (ER)–mitochondrial encounter structure (ERMES) physically links the membranes of the ER and mitochondria in yeast. Although the ER and mitochondria cooperate to synthesize glycerophospholipids, whether ERMES directly facilitates the lipid exchange between the two organelles remains controversial. Here, we compared the x-ray structures of an ERMES subunit Mdm12 from Kluyveromyces lactis with that of Mdm12 from Saccharomyces cerevisiae and found that both Mdm12 proteins possess a hydrophobic pocket for phospholipid binding. However in vitro lipid transfer assays showed that Mdm12 alone or an Mmm1 (another ERMES subunit) fusion protein exhibited only a weak lipid transfer activity between liposomes. In contrast, Mdm12 in a complex with Mmm1 mediated efficient lipid transfer between liposomes. Mutations in Mmm1 or Mdm12 impaired the lipid transfer activities of the Mdm12–Mmm1 complex and furthermore caused defective phosphatidylserine transport from the ER to mitochondrial membranes via ERMES in vitro. Therefore, the Mmm1–Mdm12 complex functions as a minimal unit that mediates lipid transfer between membranes.
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“Mdm12, Mdm34, and Mmm1 have synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domains [24], and the ERMES complex mediates lipid transport [25,26].”
From In Candida glabrata, ERMES Component GEM1 Controls Mitochondrial Morphology, mtROS, and Drug Efflux Pump Expression, Resulting in Azole Susceptibility (2023) · cites this paper as [25]
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Cites
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MethodComparison of simple potential functions for simulating liquid water
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BackgroundMethod[20] Processing of X-ray diffraction data collected in oscillation mode
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MethodPhaser crystallographic software
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“To monitor lipid transfer between liposomes via the HMmm1s– Mdm12 complex and MBP-HMmm1s, we adopted fluorescent dequenching assays as described previously (Connerth et al., 2012; Watanabe et al., 2015; Miyata et al., 2016).”
Method
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Items 101–154 of 154
Odendall, F., Backes, S., Tatsuta, T., Weill, U., Schuldiner, M., Langer, T., Herrmann, J. M., Rapaport, D., & Dimmer, K. S. (2019) · Molecular Biology of the Cell · doi:10.1091/mbc.e19-03-0166 · Cited by 8
“The main function of the ERMES complex seems to be its role in lipid exchange and it was the first mitochondrial tethering complex for which direct binding of lipid molecules was shown (AhYoung et al. , 2015; Kawano et al. , 2018).”
Ltc1 localization by EMC regulates cell membrane fluidity to facilitate membrane protein biogenesis
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“This complex forms a tether between the mitochondria and the ER that is important for lipid exchange and mitochondrial function (Xue et al., 2017; Kawano et al., 2018; Kornmann, 2020).”
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“As Mmm1 was shown to form a homodimer [3], the assembly of two channels has been proposed, in which one Mmm1 subunit interacts with Mdm12 and the second with Mmm2 (Model II) [32], or the two channels may each consist of Mmm1/Mdm12/ Mmm2 subunits (Model III) [49].”
BackgroundLipid transfer at mitochondrial membrane contact sites
Chu, Q., & Ji, W.-K. (2024) · Mitochondrial Communications · doi:10.1016/j.mitoco.2024.11.002 · Cited by 4
Exploring mitochondrial dynamics and localization under cellular stress: A comprehensive insight
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BackgroundCharacterization of Tgl2, a putative lipase in yeast mitochondriaPreprint
Tiku, V., Tatsuta, T., Jung, M., Rapaport, D., & Dimmer, K. S. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.08.593122 · Cited by 1
“The ERMES complex was the first of such mitochondrial tethers to be recognized, and has been now thoroughly elucidated (42–44).”
BackgroundFunctional analysis of membrane contact sites in C. elegans early embryogenesis
Jeyasimman, D. (2021) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/152202
Cnm1: A bridge between mitochondria and nuclear ER
Casler, J. C., & Lackner, L. L. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202109021
The structural organization and functions of the ERMES complex in fungi
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Berraquero, M., Tallada, V. A., & Jiménez, J. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.15.618411
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Metadata
- Authors
- Kawano, S., Tamura, Y., Kojima, R., Bala, S., Asai, E., Michel, A. H., Kornmann, B., Riezman, I., Riezman, H., Sakae, Y., Okamoto, Y., & Endo, T.
- Affiliations
- Kyoto Sangyo University (JP)
- Yamagata University (JP)
- Nagoya University (JP)
- ETH Zurich (CH)
- Institute of Biochemistry, ETH Zürich, Zürich, Switzerland 9
- University of Geneva (CH)
- Corresponding author
- Endo, Toshiya
- ORCID
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2017-12-26
- Volume
- 217
- Issue
- 3
- Pages
- 959-974
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC5839780
- OpenAlex
- W2777157902
- Cited by
- 148
- References
- 58
- Citations by year
- 2026: 12 · 2025: 11 · 2024: 20 · 2023: 11 · 2022: 14 · 2021: 17 · 2020: 23 · 2019: 26 · 2018: 14
- FWCI
- 8.72
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Archive ouverte UNIGE (University of Geneva) (publishedVersion, other-oa)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- Repository for Publications and Research Data (ETH Zurich) (submittedVersion, cc-by-nc-sa)
- ETH Zürich Research Collection
- Funders
- Japan Society of the Promotion of Science (25840020, 17K18230, 15H05595, 15H05705, 2222703)
- Japan Science and Technology Agency
- Core Research for Evolutional Science and Technology (JPMJCR12M1)
- Swiss National Science Foundation
- National Centre of Competence in Research
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- ERMES, lipid transfer, endoplasmic reticulum-mitochondria contacts, phosphatidylserine transport, glycerophospholipid biosynthesis, Kluyveromyces lactis, Saccharomyces cerevisiae, protein structure, membrane lipid exchange
- MeSH terms
- Biological Transport, Active, Endoplasmic Reticulum, Kluyveromyces, Membrane Proteins, Phospholipids, Saccharomyces cerevisiae, Structure-Activity Relationship, Mitochondrial Proteins, Saccharomyces cerevisiae Proteins, Multiprotein Complexes, Mitochondrial Membranes
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