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An ER-Mitochondria Tethering Complex Revealed by a Synthetic Biology Screen
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Making Connections: Endoplasmic reticulum (ER)–mitochondria connections have been implicated in many physiological processes, including calcium homeostasis, signaling, membrane biogenesis, and apoptosis. Kornmann et al. (p. 477 , published online 25 June; see the Perspective by Wiedemann et al. ) looked for a proteinaceous link between the ER and mitochondria and, using combinations of synthetic biology and classical yeast genetics, found a protein complex that tethers the two organelles. A large-scale genetic interaction map suggests that these ER-mitochondria connections are important for interorganellar phospholipid exchange.
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“The ERMES complex is composed of four core subunits: an ER-resident protein Mmm1, a cytosolic protein Mdm12, and mitochondrial outer membrane proteins Mdm10 and Mdm34 [21] (Figure 1A).”
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 [21]
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“MDM34 encodes a protein of the mitochondrial outer membrane that is a part of the ERMES complex that tethers mitochondria to the ER and is also involved in their contact with peroxisomes (Kornmann et al. 2009; Cohen et al. 2014).”
From Mitochondrial retrograde control of transcription evolves with respiratory stress, metabolic adaptation, and virulence in budding yeasts (2026) · cites this paper as Kornmann et al. 2009
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“Deletion of any four proteins of the ERMES core complex results in the impaired formation of the ERMES complex and instability of ER-mitochondrial contact [21].”
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 [21]
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“In Saccharomyces cerevisiae, the outer mitochondrial membrane is connected to the endoplasmic reticulum (ER) through the contact site formed by the ER-mitochondria encounter structure (ERMES) complex [21].”
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 [21]
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Metadata
- Authors
- Kornmann, B., Currie, E., Collins, S. R., Schuldiner, M., Nunnari, J., Weissman, J. S., & Walter, P.
- Affiliations
- Department of Biochemistry and Biophysics, University of California at San Francisco, San Francisco, CA 94158, USA.
- University of California, San Francisco (US)
- Howard Hughes Medical Institute (US)
- Weizmann Institute of Science (IL)
- University of California, Davis (US)
- Corresponding author
- Currie, Erin
- Collins, Sean R.
- Venue
- Science
- Published
- 2009-07-24
- Volume
- 325
- Issue
- 5939
- Pages
- 477-481
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC2933203
- OpenAlex
- W1997527771
- Cited by
- 1,275
- References
- 32
- Citations by year
- 2026: 29 · 2025: 49 · 2024: 79 · 2023: 54 · 2022: 63 · 2021: 91 · 2020: 86 · 2019: 89 · 2018: 80 · 2017: 85 · 2016: 90 · 2015: 74 · 2014: 91 · 2013: 88 · 2012: 73
- FWCI
- 30.30
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Science Foundation
- Howard Hughes Medical Institute
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM062942, R01GM032384)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
- Keywords
- ER-mitochondria tethering, inter-organelle communication, phospholipid synthesis, calcium signaling, genetic interaction mapping
- MeSH terms
- Animals, Endoplasmic Reticulum, Membrane Proteins, Mitochondria, Phospholipids, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Calcium Signaling, Mitochondrial Proteins, Saccharomyces cerevisiae Proteins, Mice
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