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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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Cites
Global analysis of protein expression in yeast
Ghaemmaghami, S., Huh, W.-K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., & Weissman, J. S. (2003) · Nature · doi:10.1038/nature02046 · Cited by 3,750
Self-citationMitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442
Close Contacts with the Endoplasmic Reticulum as Determinants of Mitochondrial Ca 2+ Responses
Rizzuto, R., Pinton, P., Carrington, W., Fay, F. S., Fogarty, K. E., Lifshitz, L. M., Tuft, R. A., & Pozzan, T. (1998) · Science · doi:10.1126/science.280.5370.1763 · Cited by 2,257
Hayashi, T., & Su, T.-P. (2007) · Cell · doi:10.1016/j.cell.2007.08.036 · Cited by 1,826
Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels
Szabadkai, G., Bianchi, K., Várnai, P., De Stefani, D., Wieckowski, M. R., Cavagna, D., Nagy, A. I., Balla, T., & Rizzuto, R. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200608073 · Cited by 1,413
Csordás, G., Renken, C. W., Várnai, P., Walter, L., Weaver, D., BUTTLE, K. F., Balla, T., Mannella, C. A., & Hajnóczky, G. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200604016 · Cited by 1,377
Rizzuto, R., Brini, M., Murgia, M., & Pozzan, T. (1993) · Science · doi:10.1126/science.8235595 · Cited by 1,207
Calcium and apoptosis: ER-mitochondria Ca2+ transfer in the control of apoptosis
Pinton, P., Giorgi, C., Siviero, R., Zecchini, E., & Rizzuto, R. (2008) · Oncogene · doi:10.1038/onc.2008.308 · Cited by 1,178
Rapid changes of mitochondrial Ca2+ revealed by specifically targeted recombinant aequorin
Rizzuto, R., Simpson, A. W. M., Brini, M., & Pozzan, T. (1992) · Nature · doi:10.1038/358325a0 · Cited by 931
The Mechanism of Ca2+-Dependent Regulation of Kinesin-Mediated Mitochondrial Motility
Wang, X., & Schwarz, T. L. (2009) · Cell · doi:10.1016/j.cell.2008.11.046 · Cited by 871
Schuldiner, M., Collins, S. R., Thompson, N. J., Denic, V., Bhamidipati, A., Punna, T., Ihmels, J., Andrews, B., Boone, C., Greenblatt, J. F., et al. (2005) · Cell · doi:10.1016/j.cell.2005.08.031 · Cited by 870
Self-citationPACS‐2 controls endoplasmic reticulum–mitochondria communication and Bid‐mediated apoptosis
Simmen, T., Aslan, J. E., Blagoveshchenskaya, A. D., Thomas, L., Wan, L., Xiang, Y. K., Feliciangeli, S. F., Hung, C., Crump, C. M., & Thomas, G. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600559 · Cited by 608
Hieter, P. (1985) · Cell · doi:10.1016/0092-8674(85)90152-7 · Cited by 443
Dissecting Membrane Insertion of Mitochondrial β-Barrel Proteins
Kutik, S., Stojanovski, D., Becker, L., Becker, T., Meinecke, M., Krüger, V., Prinz, C., Meisinger, C., Guiard, B., Wagner, R., et al. (2008) · Cell · doi:10.1016/j.cell.2008.01.028 · Cited by 301
Osman, C., Haag, M., Potting, C., Rodenfels, J., Dip, P. V., Wieland, F., Brügger, B., Westermann, B., & Langer, T. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200810189 · Cited by 301
Achleitner, G., Gaigg, B., Krasser, A., Kainersdorfer, E., Kohlwein, S. D., Perktold, A., Zellnig, G., & Daum, G. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00658.x · Cited by 300
Boldogh, I., Nowakowski, D. W., Yang, H.-C., Chung, H., Karmon, S., Royes, P., & Pon, L. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-04-0225 · Cited by 283
Birner‐Gruenberger, R., Bürgermeister, M., Schneiter, R., & Daum, G. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.4.997 · Cited by 269
Trotter, P. J., & Voelker, D. R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.11.6062 · Cited by 265
[14] Cloning genes by complementation in yeast
Rose, M. D., & Broach, J. R. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)94017-7 · Cited by 259
Yeast Miro GTPase, Gem1p, regulates mitochondrial morphology via a novel pathway
Frederick, R. L., McCaffery, J. M., Cunningham, K. W., Okamoto, K., & Shaw, J. M. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200405100 · Cited by 247
Vance, J. E. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)52406-6 · Cited by 214
Chang, S.-C., Heacock, P. N., Mileykovskaya, E., Voelker, D. R., & Dowhan, W. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.24.14933 · Cited by 209
Berger, K. H., Sogo, L. F., & Yaffe, M. P. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.136.3.545 · Cited by 197
Evidence for a two membrane–spanning autonomous mitochondrial DNA replisome
Meeusen, S., & Nunnari, J. M. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200304040 · Cited by 177
Self-citationTemperature-sensitive yeast mutants defective in mitochondrial inheritance.
McConnell, S. J., Stewart, L. C., Talin, A. A., & Yaffe, M. P. (1990) · The Journal of Cell Biology · doi:10.1083/jcb.111.3.967 · Cited by 167
The morphology proteins Mdm12/Mmm1 function in the major β‐barrel assembly pathway of mitochondria
Meisinger, C., Pfannschmidt, S., Rissler, M., Milenkovic, D., Becker, T., Stojanovski, D., Youngman, M. J., Jensen, R. E., Chacińska, A., Guiard, B., et al. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601673 · Cited by 157
Youngman, M. J., Hobbs, A. E. A., Burgess, S. M., Srinivasan, M., & Jensen, R. E. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200308012 · Cited by 148
Gohil, V. M., Thompson, M. N., & Greenberg, M. L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505478200 · Cited by 135
New perspectives on the regulation of intermembrane glycerophospholipid traffic
Voelker, D. R. (2003) · Journal of Lipid Research · doi:10.1194/jlr.r200020-jlr200 · Cited by 96
Diverse membrane‐associated proteins contain a novel SMP domain
Lee, I., & Hong, W. (2006) · The FASEB Journal · doi:10.1096/fj.05-4581hyp · Cited by 89
Kondo‐Okamoto, N., Shaw, J. M., & Okamoto, K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308436200 · Cited by 47
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Cited by
Sorted by citations
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Friedman, J. R., Lackner, L. L., West, M., DiBenedetto, J. R., Nunnari, J., & Voeltz, G. K. (2011) · Science · doi:10.1126/science.1207385 · Cited by 2,072
Self-citationMitochondrial form and function
Friedman, J. R., & Nunnari, J. (2014) · Nature · doi:10.1038/nature12985 · Cited by 1,803
Self-citationLi‐Beisson, Y., Shorrosh, B. S., Beisson, F., Andersson, M. X., Arondel, V., Bates, P. D., Baud, S., Bird, D. A., DeBono, A., Durrett, T. P., et al. (2013) · The Arabidopsis Book · doi:10.1199/tab.0161 · Cited by 1,575
Molecular mechanisms and physiological functions of mitophagy
Onishi, M., Yamano, K., Sato, M., Matsuda, N., & Okamoto, K. (2021) · The EMBO Journal · doi:10.15252/embj.2020104705 · Cited by 1,469
Chipuk, J. E., Moldoveanu, T., Llambi, F., Parsons, M. J., & Green, D. R. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.01.025 · Cited by 1,476
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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