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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
Flagged first, then by citations
Cited by
Sorted by citations
Items 401–500 of 1,001
Mdm10 is an ancient eukaryotic porin co-occurring with the ERMES complex
Flinner, N., Ellenrieder, L., Stiller, S. B., Becker, T., Schleiff, E., & Mirus, O. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.10.006 · Cited by 73
Singh, A., Yadav, V., & Prasad, R. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039812 · Cited by 72
Failure is not an option – mitochondrial genome segregation in trypanosomes
Schneider, A., & Ochsenreiter, T. (2018) · Journal of Cell Science · doi:10.1242/jcs.221820 · Cited by 71
Of yeast, mice and men: MAMs come in two flavors
Herrera-Cruz, M. S., & Simmen, T. (2017) · Biology Direct · doi:10.1186/s13062-017-0174-5 · Cited by 73
The Metabolic Prospective and Redox Regulation of Macrophage Polarization
He, C., & Carter, A. B. (2015) · Journal of Clinical & Cellular Immunology · doi:10.4172/2155-9899.1000371 · Cited by 74
Alignment of sarcoplasmic reticulum-mitochondrial junctions with mitochondrial contact points
Garcı́a-Pérez, C., Schneider, T. G., Hajnóczky, G., & Csordás, G. (2011) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00397.2011 · Cited by 72
Protein Carbonylation and Adipocyte Mitochondrial Function
Curtis, J. M., Hahn, W. S., Stone, M. D., Inda, J. J., Droullard, D. J., Kuzmicic, J., Donoghue, M. A., Long, E. K., Armién, A. G., Lavandero, S., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.400663 · Cited by 73
Roles of mitochondria in neutrophils
Cao, Z., Zhao, M. L., Sun, H., Hu, L., Chen, Y., & Fan, Z. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.934444 · Cited by 74
Han, F., Yan, S.-N., & Shi, Y. (2013) · PLoS ONE · doi:10.1371/journal.pone.0069340 · Cited by 70
Thomas, G., Aslan, J. E., Thomas, L., Shinde, P., Shinde, U. P., & Simmen, T. (2017) · Journal of Cell Science · doi:10.1242/jcs.199463 · Cited by 69
Li, X., Zhao, X., Qin, Z., Li, J., Sun, B., & Liu, L. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-024-02014-w · Cited by 69
Inheritance of the fittest mitochondria in yeast
Vevea, J., Swayne, T. C., Boldogh, I. R., & Pon, L. A. (2013) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.07.003 · Cited by 69
McLaughlin, J. E., Bin-Umer, M. A., Tortora, A., Mendez, N., McCormick, S. P., & Tumer, N. E. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909777106 · Cited by 69
Regulation of Mitochondrial Dynamics and Autophagy by the Mitochondria-Associated Membrane
Tagaya, M., & Arasaki, K. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-4567-7_3 · Cited by 74
Sun, E. W., Guillén-Samander, A., Bian, X., Wu, Y., Cai, Y., Messa, M., & Camilli, P. V. D. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1820156116 · Cited by 68
Hewitt, V. L., Alcock, F., & Lithgow, T. J. (2010) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2010.07.019 · Cited by 66
Mitochondrial lipid transport at a glance
Scharwey, M., Tatsuta, T., & Langer, T. (2013) · Journal of Cell Science · doi:10.1242/jcs.134130 · Cited by 74
An ER phospholipid hydrolase drives ER-associated mitochondrial constriction for fission and fusion
Nguyen, T. T., & Voeltz, G. K. (2022) · eLife · doi:10.7554/elife.84279 · Cited by 68
Redox Regulation of Store-Operated Ca 2+ Entry
Nunes, P., & Demaurex, N. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5615 · Cited by 70
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Wong, L. H., & Levine, T. P. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.05.019 · Cited by 65
Verma, S., Shakya, V. P. S., & Idnurm, A. (2018) · Virulence · doi:10.1080/21505594.2017.1414133 · Cited by 67
Identification of new channels by systematic analysis of the mitochondrial outer membrane
Krüger, V., Becker, T., Becker, L., Montilla‐Martinez, M., Ellenrieder, L., Vögtle, F. ‐., Meyer, H. E., Ryan, M. T., Wiedemann, N., Warscheid, B., et al. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201706043 · Cited by 70
Nikolaisen, J., Nilsson, L. I. H., Pettersen, I. K. N., Willems, P. H. G. M., Lorens, J. B., Koopman, W. J. H., & Tronstad, K. J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0101365 · Cited by 67
Tafesse, F., Vacaru, A. M., Bosma, E. F., Hermansson, M., Jain, A., Hilderink, A., Somerharju, P. J., & Holthuis, J. C. M. (2013) · Journal of Cell Science · doi:10.1242/jcs.138933 · Cited by 67
Herrera-Cruz, M. S., & Simmen, T. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-4567-7_2 · Cited by 68
Tucey, T. M., Verma-Gaur, J., Nguyen, J., Hewitt, V. L., Lo, T. L., Shingu-Vazquez, M., Robertson, A. A. B., Hill, J. R., Pettolino, F. A., Beddoe, T., et al. (2016) · mSphere · doi:10.1128/msphere.00074-16 · Cited by 66
“Studies in S. cerevisiae suggested roles for ERMES not only in mitochondrial morphology but also in mitochondrial lipid homeostasis, fitness, and respiration through maintenance of the mitochondrial genome (20, 27–34).”
Mueller, S. J., Lang, D., Hoernstein, S. N. W., Lang, E. G. E., Schuessele, C., Schmidt, A., Fluck, M., Leisibach, D., Niegl, C., Zimmer, A. D., et al. (2014) · PLANT PHYSIOLOGY · doi:10.1104/pp.114.235754 · Cited by 65
Processing and Topology of the Yeast Mitochondrial Phosphatidylserine Decarboxylase 1*
Horvath, S. E., Böttinger, L., Vögtle, F., Wiedemann, N., Meisinger, C., Becker, T., & Daum, G. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.398107 · Cited by 70
Gao, Y., Xiong, J., Chu, Q., & Ji, W.-K. (2021) · Journal of Cell Science · doi:10.1242/jcs.255026 · Cited by 66
Assembly of the Mitochondrial Protein Import Channel
Becker, T., Guiard, B., Thornton, N., Zufall, N., Stroud, D. A., Wiedemann, N., & Pfanner, N. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-06-0518 · Cited by 65
Satish, S., Jiménez-Ortigosa, C., Zhao, Y., Lee, M. H., Dolgov, E., Krüger, T., Park, S., Denning, D. W., Kniemeyer, O., Brakhage, A. A., et al. (2019) · mBio · doi:10.1128/mbio.00779-19 · Cited by 64
Bereiter‐Hahn, J., & Jendrach, M. (2010) · International review of cytology · doi:10.1016/s1937-6448(10)84001-8 · Cited by 67
Endoplasmic Reticulum–Mitochondria Contact Sites—Emerging Intracellular Signaling Hubs
Aoyama-Ishiwatari, S., & Hirabayashi, Y. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.653828 · Cited by 66
Miro's N-Terminal GTPase Domain Is Required for Transport of Mitochondria into Axons and Dendrites
Babić, M., Russo, G. J., Wellington, A. J., Sangston, R., Gonzalez, M., & Zinsmaier, K. E. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.1035-14.2015 · Cited by 67
Glycerolipid synthesis and lipid trafficking in plant mitochondria
Michaud, M., Prinz, W. A., & Jouhet, J. (2016) · FEBS Journal · doi:10.1111/febs.13812 · Cited by 63
Mitochondrial acyltransferases and glycerophospholipid metabolism
González-Baró, M. R., & Coleman, R. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.06.023 · Cited by 64
Molecular model of the mitochondrial genome segregation machinery in Trypanosoma brucei
Hoffmann, A., Käser, S., Jakob, M., Amodeo, S., Peitsch, C., Týč, J., Vaughan, S., Zuber, B., Schneider, A., & Ochsenreiter, T. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1716582115 · Cited by 64
Role of VPS13, a protein with similarity to ATG2, in physiology and disease
Ugur, B., Hancock-Cerutti, W., Leonzino, M., & De Camilli, P. (2020) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2020.05.027 · Cited by 73
Debattisti, V., Pendin, D., Ziviani, E., Daga, A., & Scorrano, L. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201306121 · Cited by 63
Mfn2 localization in the ER is necessary for its bioenergetic function and neuritic development
Casellas‐Díaz, S., Larramona‐Arcas, R., Riqué‐Pujol, G., Tena‐Morraja, P., Müller‐Sánchez, C., Segarra‐Mondejar, M., Gavaldà‐Navarro, A., Villarroya, F., Reina, M., Martínez-Estrada, O. M., et al. (2021) · EMBO Reports · doi:10.15252/embr.202051954 · Cited by 68
Cnm1 mediates nucleus–mitochondria contact site formation in response to phospholipid levels
Eisenberg‐Bord, M., Zung, N., Collado, J., Drwesh, L., Fenech, E. J., Fadel, A., Dezorella, N., Bykov, Y. S., Rapaport, D., Fernández‐Busnadiego, R., et al. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202104100 · Cited by 60
Self-citationPERK recruits E-Syt1 at ER–mitochondria contacts for mitochondrial lipid transport and respiration
Sassano, M. L., van Vliet, A. R., Vervoort, E., Eygen, S. V., den Haute, C. V., Pavie, B., Roels, J., Swinnen, J. V., Spinazzi, M., Moens, L., et al. (2023) · The Journal of Cell Biology · doi:10.1083/jcb.202206008 · Cited by 61
Suresh, H. G., dos Santos, A. X. D. S., Kukulski, W., Tyedmers, J., Riezman, H., Bukau, B., & Mogk, A. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-11-1559 · Cited by 63
Mechanisms of Protein Sorting in MitochondriaPreprint
Stojanovski, D., Bohnert, M., Pfanner, N., & van der Laan, M. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011320 · Cited by 63
Lipid scrambling is a general feature of protein insertases
Li, D., Rocha-Roa, C., Schilling, M. A., Reinisch, K. M., & Vanni, S. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2319476121 · Cited by 63
Mitochondrial origins of the pressure to sleep
Sarnataro, R., Velasco, C. D., Monaco, N., Kempf, A., & Miesenböck, G. (2025) · Nature · doi:10.1038/s41586-025-09261-y · Cited by 62
Organelle contact zones as sites for lipid transfer
Tamura, Y., Kawano, S., & Endo, T. (2018) · The Journal of Biochemistry · doi:10.1093/jb/mvy088 · Cited by 60
Zampese, E., & Pizzo, P. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0845-9 · Cited by 62
Wideman, J. G., Go, N. E., Klein, A., Redmond, E. L., Lackey, S. W. K., Tao, T., Kalbacher, H., Rapaport, D., Neupert, W., & Nargang, F. E. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-10-0844 · Cited by 62
ER–mitochondria contacts: Actin dynamics at the ER control mitochondrial fission via calcium release
Steffen, J., & Koehler, C. M. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201711075 · Cited by 61
Stress responsive mitochondrial proteins in Arabidopsis thaliana
Wang, Y., Berkowitz, O., Selinski, J., Xu, Y., Hartmann, A., & Whelan, J. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.03.031 · Cited by 62
The topology and regulation of cardiolipin biosynthesis and remodeling in yeast
Baile, M. G., Lu, Y., & Claypool, S. M. (2013) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2013.10.008 · Cited by 61
Peter, A. T. J., van Schie, S. N. S., Cheung, N. J., Michel, A. H., Peter, M., & Kornmann, B. (2022) · The EMBO Journal · doi:10.15252/embj.2021109998 · Cited by 59
Self-citationMitochondria-associated membranes: A hub for neurodegenerative diseases
Liu, J., & Yang, J. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.112890 · Cited by 67
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Mehlitz, A., Rajeeve, K., Herweg, J., Krohne, G., van de Linde, S., Rieck, E., Sauer, M., & Rudel, T. (2014) · Cellular Microbiology · doi:10.1111/cmi.12278 · Cited by 62
Apoptosis and the yeast actin cytoskeleton
Leadsham, J. E., Kotiadis, V. N., Tarrant, D., & Gourlay, C. W. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.196 · Cited by 63
Biosynthesis and roles of phospholipids in mitochondrial fusion, division and mitophagy
Zhang, Q., Tamura, Y., Roy, M., Adachi, Y., Iijima, M., & Sesaki, H. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1648-6 · Cited by 65
Nordzieke, S., Zobel, T., Fränzel, B., Wolters, D. A., Kück, U., & Teichert, I. (2014) · Eukaryotic Cell · doi:10.1128/ec.00241-14 · Cited by 61
Regulation of the H+-ATP synthase by IF1: a role in mitohormesis
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Escobar‐Henriques, M., & Langer, T. (2014) · EMBO Reports · doi:10.1002/embr.201338225 · Cited by 61
Genetic instability in budding and fission yeast—sources and mechanisms
Skoneczna, A., Kaniak, A., & Skoneczny, M. (2015) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuv028 · Cited by 59
Mast, F. D., Jamakhandi, A. P., Saleem, R. A., Dilworth, D. J., Rogers, R. S., Rachubinski, R. A., & Aitchison, J. D. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.728154 · Cited by 60
Generation and functions of second messengers microdomains
Filadi, R., & Pozzan, T. (2015) · Cell Calcium · doi:10.1016/j.ceca.2015.03.007 · Cited by 59
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Murcha, M. W., Wang, Y., Narsai, R., & Whelan, J. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.09.026 · Cited by 58
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Santos, H. J., Makiuchi, T., & Nozaki, T. (2018) · Trends in Parasitology · doi:10.1016/j.pt.2018.08.008 · Cited by 61
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Callegari, S., & Dennerlein, S. (2018) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2018.00031 · Cited by 58
Gong, Y., Lin, J., Ma, Z., Yu, M., Wang, M., Lai, D., & Fu, G. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119511 · Cited by 58
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Moir, R. D., Gross, D. A., Silver, D. L., & Willis, I. M. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002890 · Cited by 59
Gawryluk, R. M. R., Chisholm, K. A., Pinto, D. M., & Gray, M. W. (2014) · Journal of Proteomics · doi:10.1016/j.jprot.2014.07.005 · Cited by 55
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Dimmer, K. S., & Rapaport, D. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.07.010 · Cited by 56
Integrative functions of the mitochondrial contact site and cristae organizing system
Schorr, S., & van der Laan, M. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.09.021 · Cited by 56
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Gutiérrez, T., Qi, H., Yap, M. C., Tahbaz, N., Milburn, L., Lucchinetti, E., Lou, P., Zaugg, M., LaPointe, P., Mercier, P., et al. (2020) · Science Signaling · doi:10.1126/scisignal.aax6660 · Cited by 57
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Petković, M., O’Brien, C. E., & Jan, Y. N. (2021) · Genes & Development · doi:10.1101/gad.346759.120 · Cited by 58
Qu, Y., Jelicic, B., Pettolino, F., Perry, A., Lo, T. L., Hewitt, V. L., Bantun, F., Beilharz, T. H., Peleg, A. Y., Lithgow, T., et al. (2012) · Eukaryotic Cell · doi:10.1128/ec.05292-11 · Cited by 57
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Horvath, S. E., Rampelt, H., Oeljeklaus, S., Warscheid, B., van der Laan, M., & Pfanner, N. (2014) · Protein Science · doi:10.1002/pro.2625 · Cited by 61
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Mbuyane, L. L., Bauer, F. F., & Divol, B. (2021) · Food Research International · doi:10.1016/j.foodres.2021.110142 · Cited by 62
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An, G., Park, J., Song, J., Hong, T., Song, G., & Lim, W. (2024) · Experimental & Molecular Medicine · doi:10.1038/s12276-023-01137-3 · Cited by 57
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Nakamura, K., Aoyama-Ishiwatari, S., Nagao, T., Paraan, M., Obara, C. J., Sakurai-Saito, Y., Johnston, J. D., Du, Y., Suga, S., Tsuboi, M., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-58538-3 · Cited by 69
Itoh, K., Tamura, Y., Iijima, M., & Sesaki, H. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-03-0125 · Cited by 58
Horibata, Y., Ando, H., Zhang, P., Vergnes, L., Aoyama, C., Itoh, M., Reue, K., & Sugimoto, H. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.736793 · Cited by 52
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Harsman, A., & Schneider, A. (2016) · Traffic · doi:10.1111/tra.12463 · Cited by 55
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Xue, Y., Schmollinger, S., Attar, N., Campos, O. A., Vogelauer, M., Carey, M., Merchant, S., & Kurdistani, S. K. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.784249 · Cited by 58
Tsui, H. S., Pham, N. B., Amer, B. R., Bradley, M. C., Gosschalk, J. E., Gallagher-Jones, M., Ibarra, H., Clubb, R., Blaby, C., & Clarke, C. F. (2019) · Journal of Lipid Research · doi:10.1194/jlr.m093534 · Cited by 57
Current and Emerging Approaches for Studying Inter-Organelle Membrane Contact Sites
Huang, X. S., Jiang, C., Yu, L., & Yang, A. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00195 · Cited by 62
Zhang, P., Konja, D., Zhang, Y., & Wang, Y. (2021) · Cells · doi:10.3390/cells10092195 · Cited by 58
Schnarwiler, F., Niemann, M., Doiron, N., Harsman, A., Käser, S., Mani, J., Chanfon, A., Dewar, C. E., Oeljeklaus, S., Jackson, C. B., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1404854111 · Cited by 49
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Bubulya, P. A. (2012) · InTech eBooks · doi:10.5772/1081 · Cited by 57
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Peter, A. T. J., Petrungaro, C., Peter, M., & Kornmann, B. (2022) · Nature Cell Biology · doi:10.1038/s41556-022-00917-9 · Cited by 56
Self-citationYoda, E., Hachisu, K., Taketomi, Y., Yoshida, K., Nakamura, M., Ikeda, K., Taguchi, R., Nakatani, Y., Kuwata, H., Murakami, M., et al. (2010) · Journal of Lipid Research · doi:10.1194/jlr.m008060 · Cited by 55
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Kopec, K. O., Alva, V., & Lupas, A. N. (2011) · Biochemical Society Transactions · doi:10.1042/bst0391033 · Cited by 54
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Mesmin, B. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201606069 · Cited by 54
Outer membrane protein functions as integrator of protein import and DNA inheritance in mitochondria
Käser, S., Oeljeklaus, S., Týč, J., Vaughan, S., Warscheid, B., & Schneider, A. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1605497113 · Cited by 54
Ubiquitination of ERMES components by the E3 ligase Rsp5 is involved in mitophagy
Belgareh‐Touzé, N., Cavellini, L., & Cohen, M. M. (2016) · Autophagy · doi:10.1080/15548627.2016.1252889 · Cited by 54
Fowler, P. C., Garcia-Pardo, M. E., Simpson, J. C., & O’Sullivan, N. C. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01051 · Cited by 53
Gao, P., Yang, W., & Sun, L. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/3120539 · Cited by 58
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Huang, J., Meng, P., Wang, C., Zhang, Y., & Zhou, L. (2022) · Theranostics · doi:10.7150/thno.70588 · Cited by 54
Key challenges and recommendations for defining organelle membrane contact sites
Calí, T., Bayer, E., Eden, E. R., Hajnóczky, G., Kornmann, B., Lackner, L. L., Liou, J., Reinisch, K. M., Rhee, H., Rizzuto, R., et al. (2025) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-025-00864-x · Cited by 65
Self-citationTo, T., Fadul, M. J., & Shu, X. (2014) · Nature Communications · doi:10.1038/ncomms5072 · Cited by 54
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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