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Endoplasmic reticulum-mitochondria contacts: Function of the junction
Open accessAbstract
The most well-characterized organelle contact sites are those between the endoplasmic reticulum (ER) and mitochondria. Increased understanding is being gained of how ER-mitochondria contact sites are organized and which factors converge at this interface, some of which may provide a tethering function. The role of the ER-mitochondria junction in coordinating the functions of these two organelles is also becoming clearer, and it has been shown to be involved in the regulation of lipid synthesis, Ca(2+) signalling and the control of mitochondrial biogenesis and intracellular trafficking.
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“Besides controlling Ca2+ flux, MAM participate in lipid synthesis, membrane stability, mitochondrial dynamics, and ROS signaling [99–101].”
From Neuronal Apolipoprotein E4 Expression Results in Proteome-Wide Alterations and Compromises Bioenergetic Capacity by Disrupting Mitochondrial Function (2019) · cites this paper as [99]
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“Mitochondria shared greater location similarity with the ER (SEC61β and SERCA) than any other structures, consistent with the functional interactions between these cellular structures22,23.”
From Integrated intracellular organization and its variations in human iPS cells (2023) · cites this paper as [22]
In the citing paper
“MAMs play a vital role in lipid transport, Ca2+ signaling, cell survival, and energy metabolism [234], and have been implicated in diseases including Alzheimer’s disease [235], cancer [236], lysosomal storage disease [237], diabetes mellitus [238,239], obesity, and metabolic disorders [240].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [234]
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Citations
Cites
Membrane lipids: where they are and how they behave
van Meer, G., Voelker, D. R., & Feigenson, G. W. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2330 · Cited by 7,157
Mitochondria: In Sickness and in Health
Nunnari, J., & Suomalainen, A. (2012) · Cell · doi:10.1016/j.cell.2012.02.035 · Cited by 3,479
Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601
Mitofusin 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
ER Tubules Mark Sites of Mitochondrial Division
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 · cited 10×
“inositol 1,4,5-trisphosphate receptor (Ins(1,4,5)P 3 R) on the ER membrane, and Ca”
InfluentialSelf-citationA forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter
Stefani, D. D., Raffaello, A., Teardo, E., Szabó, I., & Rizzuto, R. (2011) · Nature · doi:10.1038/nature10230 · Cited by 1,957
Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter
Baughman, J. M., Perocchi, F., Girgis, H. S., Plovanich, M., Belcher-Timme, C. A., Sancak, Y., Bao, X. R., Strittmatter, L., Goldberger, O., Bogorad, R. L., et al. (2011) · Nature · doi:10.1038/nature10234 · Cited by 1,953
Dynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
Smirnova, E., Griparić, L., Shurland, D., & van der Bliek, A. M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2245 · Cited by 1,938
Mitochondria as sensors and regulators of calcium signalling
Rizzuto, R., De Stefani, D., Raffaello, A., & Mammucari, C. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3412 · Cited by 1,781
Flagged first, then by citations
Cited by
Sorted by citations
Mitochondrial form and function
Friedman, J. R., & Nunnari, J. (2014) · Nature · doi:10.1038/nature12985 · Cited by 1,803
Innate Immune Pattern Recognition: A Cell Biological Perspective
Brubaker, S. W., Bonham, K. S., Zanoni, I., & Kagan, J. C. (2015) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032414-112240 · Cited by 1,475
“An interesting feature of mitochondrial and peroxisomal biology is that these organelles interact at the MAM, a specialized subdomain of the endoplasmic reticulum (26, 208).”
The autophagosome: origins unknown, biogenesis complex
Lamb, C. A., Yoshimori, T., & Tooze, S. A. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3696 · Cited by 1,371
13 reasons why the brain is susceptible to oxidative stress
Cobley, J. N., Fiorello, M. L., & Bailey, D. M. (2018) · Redox Biology · doi:10.1016/j.redox.2018.01.008 · Cited by 1,215
“dria contacts, termed ER associated mitochondria membranes (MAM [48,49]), leading to mitochondrial Ca uptake.”
BackgroundMitochondrial dysfunction in cell senescence and aging
Miwa, S., Kashyap, S., Chini, E., & von Zglinicki, T. (2022) · Journal of Clinical Investigation · doi:10.1172/jci158447 · Cited by 1,061
Bax, Bak and beyond — mitochondrial performance in apoptosis
Peña‐Blanco, A., & García‐Sáez, A. J. (2017) · FEBS Journal · doi:10.1111/febs.14186 · Cited by 987
Horvath, S. E., & Daum, G. (2013) · Progress in Lipid Research · doi:10.1016/j.plipres.2013.07.002 · Cited by 943
Mechanisms of Mitochondrial Fission and FusionPreprint
van der Bliek, A. M., Shen, Q., & Kawajiri, S. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011072 · Cited by 903
A new pathway for mitochondrial quality control: Mitochondrial-derived vesicles
Sugiura, A., McLelland, G., Fon, E. A., & McBride, H. M. (2014) · The EMBO Journal · doi:10.15252/embj.201488104 · Cited by 862
“It is now clear that there is extensive biochemical cross talk between organelles, but the mechanisms are only beginning to emerge (Sheftel et al, 2007; Zehmer et al, 2009; Rowland & Voeltz, 2012; Mesmin et al, 2013).”
BackgroundCasares, D., Escribá, P. V., & Rosselló, C. A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092167 · Cited by 863
Arruda, A. P., Pers, B. M., Parlakgül, G., Güney, E., Inouye, K., & Hotamışlıgil, G. S. (2014) · Nature Medicine · doi:10.1038/nm.3735 · Cited by 741
MAM (mitochondria-associated membranes) in mammalian cells: Lipids and beyond
Vance, J. E. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.11.014 · Cited by 625
Mitochondrial dysfunction in diabetic kidney disease
Forbes, J. M., & Thorburn, D. R. (2018) · Nature Reviews Nephrology · doi:10.1038/nrneph.2018.9 · Cited by 645
Stoica, R., Vos, K. J. D., Paillusson, S., Mueller, S., Sancho, R. M., Lau, K., Vizcay‐Barrena, G., Lin, W.-L., Xu, Y.-F., Lewis, J. M., et al. (2014) · Nature Communications · doi:10.1038/ncomms4996 · Cited by 652
“Thus ER-mitochondrial Ca 2+ exchange following release from ER stores affects both cellular Ca 2+ homeostasis and mitochondrial ATP production since several mitochondrial dehyrogenase enzymes involved in ATP synthesis are Ca 2+ regulated 4,45 .”
InfluentialMitofusin 2 ablation increases endoplasmic reticulum–mitochondria coupling
Filadi, R., Greotti, E., Turacchio, G., Luini, A., Pozzan, T., & Pizzo, P. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1504880112 · Cited by 593
“, for lipid metabolism and modulation of Ca signaling (1, 2).”
BackgroundMitochondria functionality and sperm quality
Amaral, A., Lourenço, B., Marques, M., & Ramalho‐Santos, J. (2013) · Reproduction · doi:10.1530/rep-13-0178 · Cited by 578
“Finally, the functional importance of mitochondrial connections to other organelles (such as the endoplasmic reticulum) and the cytoskeleton is gaining attention, as it may help to integrate distinct cellular functions (Anesti & Scorrano 2006, Rowland & Voeltz 2012).”
BackgroundMitofusin 2 in POMC neurons connects ER stress with leptin resistance and energy imbalance
Schneeberger, M., Dietrich, M. O., Sebastián, D., Imbernón, M., Castaño, C., Garcia, A., Esteban, Y., Gonzalez-Franquesa, A., Rodríguez, I. C., Bortolozzi, A., et al. (2013) · Cell · doi:10.1016/j.cell.2013.09.003 · Cited by 519
Melatonin and endoplasmic reticulum stress: relation to autophagy and apoptosis
Fernández, A., Ordóñez, R., Reiter, R. J., González‐Gallego, J., & Mauriz, J. L. (2015) · Journal of Pineal Research · doi:10.1111/jpi.12264 · Cited by 516
“Moreover, ER has been implicated in the regulation of various pathways such as activation of different transcriptional cascades that regulate the luminal chaperones for folding and packing of secretory proteins, intracellular trafficking, mitochondrial biogenesis, autophagy, apoptosis, and inflammation [2, 3, 5].”
BackgroundMitochondrial Dysfunction in Cancer
Boland, M. L., Chourasia, A. H., & Macleod, K. F. (2013) · Frontiers in Oncology · doi:10.3389/fonc.2013.00292 · Cited by 521
“While VDACs are readily permeable to Ca2+ at the OMM and interact with Ins(1,4,5)P3Rs at the ER (254, 255), it has been suggested that levels and activity of VDAC may regulate the amount of Ca2+ that crosses the OMM (256).”
BackgroundThe endoplasmic reticulum–mitochondria connection: One touch, multiple functions
Marchi, S., Patergnani, S., & Pinton, P. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.10.015 · Cited by 475
“and thus “tether” the two organelles [6].”
ER-mitochondria tethering by PDZD8 regulates Ca 2+ dynamics in mammalian neurons
Hirabayashi, Y., Kwon, S., Paek, H., Pernice, W. M., Paul, M. A., Lee, J., Erfani, P., Raczkowski, A. M., Petrey, D. S., Pon, L. A., et al. (2017) · Science · doi:10.1126/science.aan6009 · Cited by 505
Imaging intraorganellar Ca2+ at subcellular resolution using CEPIA
Suzuki, J., Kanemaru, K., Ishii, K., Ohkura, M., Okubo, Y., & Iino, M. (2014) · Nature Communications · doi:10.1038/ncomms5153 · Cited by 496
New insights into the function and regulation of mitochondrial fission
Otera, H., Ishihara, N., & Mihara, K. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.02.002 · Cited by 501
“A recent report demonstrated that mitochondrial division occurs at points where endoplasmic reticulum (ER) tubules wrap around the mitochondria and mark mitochondrial division sites [58 – 60].”
BackgroundContacts between the endoplasmic reticulum and other membranes in neurons
Wu, Y., Whiteus, C., Xu, C. S., Hayworth, K. J., Weinberg, R. J., Hess, H. F., & Camilli, P. V. D. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1701078114 · Cited by 489
“MCSs were defined as membrane appositions where the distance E4860 | www.pnas.org/cgi/doi/10.1073/pnas.1701078114 Wu et al. between two bilayers was ≤30 nm (8, 38–40).”
BackgroundInfluentialA proximity-dependent biotinylation map of a human cell
Go, C. D., Knight, J. D. R., Rajasekharan, A., Rathod, B., Hesketh, G. G., Abe, K. T., Youn, J., Samavarchi‐Tehrani, P., Zhang, H., Zhu, L. Y., et al. (2021) · Nature · doi:10.1038/s41586-021-03592-2 · Cited by 456
There's Something Wrong with my MAM; the ER–Mitochondria Axis and Neurodegenerative Diseases
Paillusson, S., Stoica, R., Gomez-Suaga, P., Lau, D. H. W., Mueller, S., Miller, T., & Miller, C. C. J. (2016) · Trends in Neurosciences · doi:10.1016/j.tins.2016.01.008 · Cited by 439
“However, excessive uptake of Ca by mitochondria can lead to opening of the mitochondrial permeability transition pore and signalling for apoptosis [19].”
BackgroundRIG-I and Other RNA Sensors in Antiviral Immunity
Chow, K. T., Gale, M., & Loo, Y. (2018) · Annual Review of Immunology · doi:10.1146/annurev-immunol-042617-053309 · Cited by 432
Intercellular mitochondrial transfer as a means of tissue revitalization
Liu, D., Gao, Y., Liu, J., Huang, Y., Yin, J., Feng, Y., Shi, L., Meloni, B. P., Zhang, C., Zheng, M., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00440-z · Cited by 403
Nam, J. S., Kang, M., Kang, J., Park, S., Lee, S. J. C., Kim, H., Seo, J. K., Kwon, O., Lim, M. H., Rhee, H., et al. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b05302 · Cited by 420
Tubbs, E., Theurey, P., Vial, G., Bendridi, N., Bravard, A., Chauvin, M.-A., Ji-Cao, J., Zoulim, F., Bartosch, B., Ovize, M., et al. (2014) · Diabetes · doi:10.2337/db13-1751 · Cited by 411
“The contacts between ER and mitochondria, known as mitochondria-associated ER membranes (MAMs), play a pivotal role in calcium (Ca) signaling, lipid transport, energy metabolism, and cell survival (1).”
BackgroundThe ER-Mitochondria Tethering Complex VAPB-PTPIP51 Regulates Autophagy
Gómez‐Suaga, P., Paillusson, S., Stoica, R., Noble, W. J., Hanger, D. P., & Miller, C. C. J. (2017) · Current Biology · doi:10.1016/j.cub.2016.12.038 · Cited by 424
“The tight contacts between ER and mitochondria at MAM facilitate this exchange because they enable high local concentrations of Ca (Ca puffs) to be achieved, which are sufficient to drive a response at the mitochondrial surface [6, 7].”
BackgroundMethodInfluentialCell biology of the mitochondrion
van der Bliek, A. M., Sedensky, M. M., & Morgan, P. G. (2017) · Genetics · doi:10.1534/genetics.117.300262 · Cited by 388
Aguirre, S., Luthra, P., Sánchez-Aparicio, M. T., Maestre, A. M., Patel, J. R., Lamothe, F., Fredericks, A. C., Tripathi, S., Zhu, T., Silva, J. P., et al. (2017) · Nature Microbiology · doi:10.1038/nmicrobiol.2017.37 · Cited by 393
Hung, V., Lam, S. S., Udeshi, N. D., Svinkina, T., Guzman, G., Mootha, V. K., Carr, S. A., & Ting, A. Y. (2017) · eLife · doi:10.7554/elife.24463 · Cited by 373
Paillusson, S., Gómez‐Suaga, P., Stoica, R., Little, D., Gissen, P., Devine, M. J., Noble, W. J., Hanger, D. P., & Miller, C. C. J. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1704-z · Cited by 384
“These include VDAC, mitochondrial ATP synthase and TOM20 [22, 56, 69].”
InfluentialA current perspective of autophagosome biogenesis
Shibutani, S., & Yoshimori, T. (2013) · Cell Research · doi:10.1038/cr.2013.159 · Cited by 368
Wu, W., Lin, C., Wu, K., Jiang, L., Wang, X., Li, W., Zhuang, H., Zhang, X., Chen, H. H., Li, S., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201593102 · Cited by 370
“The mitochondria-associated membrane (MAM) connects the ER with mitochondria (Rowland & Voeltz, 2012; Kornmann, 2013; Klecker et al , 2014; Marchi et al , 2014).”
Split-TurboID enables contact-dependent proximity labeling in cells
Cho, K. F., Branon, T. C., Rajeev, S., Svinkina, T., Udeshi, N. D., Thoudam, T., Kwak, C. S., Rhee, H., Lee, I., Carr, S. A., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1919528117 · Cited by 376
New functions of mitochondria associated membranes in cellular signaling
van Vliet, A. R., Verfaillie, T., & Agostinis, P. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.03.009 · Cited by 353
Calcium Homeostasis and Organelle Function in the Pathogenesis of Obesity and Diabetes
Arruda, A. P., & Hotamışlıgil, G. S. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.06.010 · Cited by 352
“Review 2009; Rowland and Voeltz, 2012).”
Manor, U., Bartholomew, S. R., Golani, G., Christenson, E. T., Kozlov, M. M., Higgs, H. N., Spudich, J. A., & Lippincott‐Schwartz, J. (2015) · eLife · doi:10.7554/elife.08828 · Cited by 342
Mechanisms and Morphology of Cellular Injury, Adaptation, and Death
MILLER, M. A., & Zachary, J. F. (2017) · Elsevier eBooks · doi:10.1016/b978-0-323-35775-3.00001-1 · Cited by 369
Mitochondrial Respiration Controls Lysosomal Function during Inflammatory T Cell Responses
Baixauli, F., Acín‐Pérez, R., Villarroya‐Beltri, C., Mazzeo, C., Núñez‐Andrade, N., Gabandé‐Rodríguez, E., Ledesma, M. D., Blázquez, A., Martín, M. A., Falcón‐Pérez, J. M., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.07.020 · Cited by 331
“Moreover, the crosstalk of mitochondria with other intracellular organelles is crucial during cell adaptation to stresses and for the preservation of organelle functionality (Rowland and Voeltz, 2012).”
Determinants and Functions of Mitochondrial Behavior
Labbè, K., Murley, A., & Nunnari, J. M. (2014) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101011-155756 · Cited by 324
Wu, S., Lu, Q., Wang, Q., Ding, Y., Ma, Z., Mao, X., Huang, K., Xie, Z., & Zou, M.-H. (2017) · Circulation · doi:10.1161/circulationaha.117.030235 · Cited by 320
CerS6-Derived Sphingolipids Interact with Mff and Promote Mitochondrial Fragmentation in Obesity
Hammerschmidt, P., Ostkotte, D., Nolte, H., Gerl, M. J., Jaïs, A., Brunner, H. L., Sprenger, H., Awazawa, M., Nicholls, H. T., Turpin-Nolan, S. M., et al. (2019) · Cell · doi:10.1016/j.cell.2019.05.008 · Cited by 314
Calcium signaling at the endoplasmic reticulum: fine-tuning stress responses
Carreras‐Sureda, A., Pihán, P., & Hetz, C. A. (2017) · Cell Calcium · doi:10.1016/j.ceca.2017.08.004 · Cited by 331
“Calcium uptake by the mitochondria exhibits different functions depending on the intensity and pattern of the signaling [78,84].”
Backgroundp53 at the endoplasmic reticulum regulates apoptosis in a Ca 2+ -dependent manner
Giorgi, C., Bonora, M., Sorrentino, G., Missiroli, S., Poletti, F., Suski, J. M., Ramírez, F. G., Rizzuto, R., Virgilio, F. D., Zito, E., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1410723112 · Cited by 320
“ER–mitochondrial cross-talk is fundamental for the upregulation of mitochondrial metabolism in stimulated cells (11) and plays a key role in decoding Ca-mediated apoptotic signals (12– 16).”
BackgroundHu, C., Huang, Y., & Li, L. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18010144 · Cited by 302
“In general, when ER starts to encircle the mitochondria, the mitochondria immediately divide and mitochondrial fission factor (Mff)-dependent Drp1 assembly is subsequently initiated [16].”
BackgroundWu, S., Lu, Q., Ding, Y., Wu, Y., Qiu, Y., Wang, P., Mao, X., Huang, K., Xie, Z., & Zou, M.-H. (2019) · Circulation · doi:10.1161/circulationaha.118.033552 · Cited by 298
Carreras‐Sureda, A., Jaña, F., Urra, H., Durand, S., Mortenson, D. E., Sagredo, A. I., Bustos, G., Hazari, Y., Ramos‐Fernández, E., Sassano, M. L., et al. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0329-y · Cited by 299
AMPK, Mitochondrial Function, and Cardiovascular Disease
Wu, S., & Zou, M.-H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21144987 · Cited by 286
“MAMs play a vital role in lipid transport, Ca2+ signaling, cell survival, and energy metabolism [234], and have been implicated in diseases including Alzheimer’s disease [235], cancer [236], lysosomal storage disease [237], diabetes mellitus [238,239], obesity, and metabolic disorders [240].”
BackgroundLegionella and Coxiella effectors: strength in diversity and activity
Qiu, J., & Luo, Z. (2017) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2017.67 · Cited by 266
Stoica, R., Paillusson, S., Gómez‐Suaga, P., Mitchell, J. C., Lau, D. H. W., Gray, E. H., Sancho, R. M., Vizcay‐Barrena, G., Vos, K. J. D., Shaw, C. E., et al. (2016) · EMBO Reports · doi:10.15252/embr.201541726 · Cited by 269
“ER–mitochondria associations control Ca exchange between the two organelles, and this can impact upon the ability of mitochondria to generate ATP [1,45].”
Rieusset, J. (2018) · Cell Death & Disease · doi:10.1038/s41419-018-0416-1 · Cited by 248
Structure, function, and regulation of mitofusin‐2 in health and disease
Chandhok, G., Lazarou, M., & Neumann, B. (2017) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12378 · Cited by 263
“…fundamental cellular events are linked to ER–mitochondria interactions such as cell proliferation, death, autophagy, calcium signalling, biogenesis, lipid metabolism, unfolded protein response (UPR), and inflammation (Rizzuto et al., 1998; Bravo et al., 2012; Rowland & Voeltz, 2012; Vance, 2014).”
BackgroundOrganelle-specific initiation of cell death
Galluzzi, L., Bravo-San Pedro, J. M., & Kroemer, G. (2014) · Nature Cell Biology · doi:10.1038/ncb3005 · Cited by 239
Alzheimer’s Disease: From Firing Instability to Homeostasis Network Collapse
Frère, S. G. A., & Slutsky, I. (2018) · Neuron · doi:10.1016/j.neuron.2017.11.028 · Cited by 242
Filadi, R., Theurey, P., & Pizzo, P. (2017) · Cell Calcium · doi:10.1016/j.ceca.2017.01.003 · Cited by 247
Lepretti, M., Martucciello, S., Burgos Aceves, M., Putti, R., & Lionetti, L. (2018) · Nutrients · doi:10.3390/nu10030350 · Cited by 232
“The contact between mitochondria and ER is known as mitochondria associated ER membrane (MAM) and is responsible for efficient communication between these organelles exchanging calcium ions, lipids, and other metabolites to maintain cellular metabolism and integrity [71].”
BackgroundThe role of Ubiquitination in Apoptosis and Necroptosis
Roberts, J. Z., Crawford, N., & Longley, D. B. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-021-00922-9 · Cited by 239
“Although RNF183 is usually localised to the ER and Bcl-xL to the mitochondria, the mitochondria and ER frequently come into close proximity and form membrane contact sites [46].”
BackgroundThe role of endoplasmic reticulum stress in neurodegenerative disease
Xiang, C., Wang, Y., Zhang, H., & Han, F. (2016) · APOPTOSIS · doi:10.1007/s10495-016-1296-4 · Cited by 235
Zebrafish models of human motor neuron diseases: Advantages and limitations
Babin, P. J., Goizet, C., & Raldúa, D. (2014) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2014.03.001 · Cited by 246
Loss of Miro1-directed mitochondrial movement results in a novel murine model for neuron disease
Nguyen, T., Oh, S. S., Weaver, D., Lewandowska, A., Maxfield, D., Schuler, M.-H., Smith, N. K., Macfarlane, J. L., Saunders, G. W., Palmer, C. A., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402449111 · Cited by 223
“In particular, physical connections between the ER membrane and the outer mitochondrial membrane are known to coordinate the functions of these organelles in many organisms (52).”
BackgroundA Cell’s Fate: An Overview of the Molecular Biology and Genetics of Apoptosis
Cavalcante, G. C., Schaan, A. P., Cabral, G. F., Santana-da-Silva, M. N., Pinto, P., Vidal, A. F., & Ribeiro‐dos‐Santos, Â. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20174133 · Cited by 233
“This permeabilization is also controlled by certain mitochondrial dynamics, which involve regulation of the organelle’s fission (mediated by Dynamin-related protein 1) [127], fusion of the outer membrane (role played by Optic atrophy 1) [128], lipid content (such as ceramides) [129], and interaction with the endoplasm…”
BackgroundEndoplasmic reticulum–associated degradation regulates mitochondrial dynamics in brown adipocytes
Zhou, Z., Torres, M., Sha, H., Halbrook, C. J., den Bergh, F. V., Reinert, R. B., Yamada, T., Wang, S., Luo, Y., Hunter, A. H., et al. (2020) · Science · doi:10.1126/science.aay2494 · Cited by 219
Eisner, V., Csordás, G., & Hajnóczky, G. (2013) · Journal of Cell Science · doi:10.1242/jcs.093609 · Cited by 219
“…in a cell-free system that consisted of microsomes and mitochondria (Voelker, 1989) and by the subsequent demonstration of interorganellar phospholipid transfer between the ER and mitochondria (Ardail et al., 1993; Gaigg et al., 1995; for a recent review see Rowland and Voeltz, 2012).”
BackgroundMitochondria, energy, and metabolism in neuronal health and disease
Trigo, D., Avelar, C., Fernandes, M., Sá, J., & Silva, O. A. B. D. C. E. (2022) · FEBS Letters · doi:10.1002/1873-3468.14298 · Cited by 225
Membrane dynamics in autophagosome biogenesis
Carlsson, S. R., & Simonsen, A. (2015) · Journal of Cell Science · doi:10.1242/jcs.141036 · Cited by 222
“PtdEtn is also shuttled from mitochondria to ER, through mitochondria–ER contact sites, and can be delivered efficiently from there to other organelles (Rowland and Voeltz, 2012).”
BackgroundAssociation of blood lipids with Alzheimer's disease: A comprehensive lipidomics analysis
Proitsi, P., Kim, M. G., Whiley, L., Simmons, A., Sattlecker, M., Velayudhan, L., Lupton, M. K., Soininen, H., Kłoszewska, I., Mecocci, P., et al. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.08.003 · Cited by 206
Regulation of ER-mitochondria contacts by Parkin via Mfn2
Basso, V., Marchesan, E., Peggion, C., Chakraborty, J., von Stockum, S., Giacomello, M., Ottolini, D., Debattisti, V., Caicci, F., Tasca, E., et al. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.09.006 · Cited by 217
Organelle-Specific Initiation of Autophagy
Sica, V., Galluzzi, L., Bravo-San Pedro, J. M., Izzo, V., Maiuri, M. C., & Kroemer, G. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.07.021 · Cited by 205
“…accumulating viral nucleic acids promote the secretion of type I interferon (IFN) upon the activation of pattern recognition receptors (PRRs) that are localized at the interface between mitochondria and the ER, the so-called mitochondria-associated ER membranes (MAMs) (Rowland and Voeltz, 2012).”
BackgroundInfluentialThe multifaceted regulation of mitophagy by endogenous metabolites
Zhang, T., Liu, Q., Gao, W., Sehgal, S. A., & Wu, H. (2021) · Autophagy · doi:10.1080/15548627.2021.1975914 · Cited by 209
“MAM is important for rapid exchange of biological molecules between mitochondria and ER to fulfill the diverse signaling transduction [88].”
BackgroundTubbs, E., Chanon, S., Robert, M., Bendridi, N., Bidaux, G., Chauvin, M.-A., Ji-Cao, J., Durand, C., Gauvrit-Ramette, D., Vidal, H., et al. (2018) · Diabetes · doi:10.2337/db17-0316 · Cited by 202
“Indeed, mitochondria and ER interact at contact points, called mitochondria-associated ER membranes (MAMs), to exchange calcium (Ca) and lipids, thus regulating cell metabolism and fate (4,5).”
BackgroundMitochondria Associated Membranes (MAMs): Architecture and physiopathological role
Barazzuol, L., Giamogante, F., & Calí, T. (2021) · Cell Calcium · doi:10.1016/j.ceca.2020.102343 · Cited by 213
STED super-resolution microscopy reveals an array of MINOS clusters along human mitochondria
Jans, D. C., Wurm, C. A., Riedel, D., Wenzel, D., Stagge, F., Deckers, M., Rehling, P., & Jakobs, S. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301820110 · Cited by 197
Mechanisms of MAVS Regulation at the Mitochondrial Membrane
Jacobs, J. L., & Coyne, C. B. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.10.007 · Cited by 203
“In addition to regulating mitochondrial fusion, MFN2 is also important in the tethering of the mitochondria to the ER at the MAM.”
BackgroundInfluentialBarriers to the free diffusion of proteins and lipids in the plasma membrane
Trimble, W. S., & Grinstein, S. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201410071 · Cited by 210
“The endoplasmic reticulum is increasingly appreciated to form intimate contacts with the plasma membrane (Carrasco and Meyer, 2011), and with the membranes of other organelles as well (Rowland and Voeltz, 2012; Hönscher and Ungermann, 2014).”
BackgroundER–endosome contact sites: molecular compositions and functions
Raiborg, C., Wenzel, E. M., & Stenmark, H. (2015) · The EMBO Journal · doi:10.15252/embj.201591481 · Cited by 202
“Certain lipid biosynthetic pathways require cooperations between enzyme complexes located in mitochondria and the ER, and contact site-mediated lipid transfer plays an important role in this context (Rowland & Voeltz, 2012).”
Untangling the web: Mechanisms underlying ER network formation
Goyal, U. D., & Blackstone, C. D. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.04.009 · Cited by 189
“Organelle interactionswith the ER are a focus of another review in this volume aswell as several other recent reviews, andwon't be discussed further here [4,18].”
ResultCelardo, I., Costa, A. C., Lehmann, S., Jones, C., Wood, N. W., Mencacci, N. E., Mallucci, G. R., Loh, S. H. Y., & Martins, L. M. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.173 · Cited by 183
Zhao, Y., Luo, L., Xu, J., Xin, P., Guo, H., Wu, J., Bai, L., Wang, G., Chu, J., Zuo, J., et al. (2018) · Cell Research · doi:10.1038/s41422-018-0024-8 · Cited by 181
Modi, S., López‐Doménech, G., Halff, E. F., Covill‐Cooke, C., Ivankovic, D., Melandri, D., Arancibia‐Cárcamo, I. L., Burden, J. J., Lowe, A. R., & Kittler, J. T. (2019) · Nature Communications · doi:10.1038/s41467-019-12382-4 · Cited by 189
Inflammation and Oxidative Stress in Chronic Kidney Disease and Dialysis Patients
Ebert, T., Neytchev, O., Witasp, A., Kublickiene, K. R., Stenvinkel, P., & Shiels, P. G. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8184 · Cited by 197
The different facets of organelle interplay—an overview of organelle interactions
Schrader, M., Godinho, L. F., Costello, J. L., & Islinger, M. (2015) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2015.00056 · Cited by 181
“…do not seem to be frequently directly connected to the plasma membrane but appear to be linked via discrete ER-cisternae (Csordás et al., 2010) or filamentous adherence plaques associated to additional vesicular structures along neuronal synapses (Spirou et al., 1998; Rowland et al., 2000).”
BackgroundRampelt, H., Zerbes, R. M., van der Laan, M., & Pfanner, N. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.05.020 · Cited by 174
Mammalian oocytes store mRNAs in a mitochondria-associated membraneless compartment
Cheng, S., Altmeppen, G., So, C., Welp, L. M., Penir, S. M. U., Ruhwedel, T., Menelaou, K., Harasimov, K., Stützer, A., Blayney, M. L., et al. (2022) · Science · doi:10.1126/science.abq4835 · Cited by 173
Theurey, P., Tubbs, E., Vial, G., Jacquemetton, J., Bendridi, N., Chauvin, M.-A., Alam, M. R., Le Romancer, M., Vidal, H., & Rieusset, J. (2016) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjw004 · Cited by 175
“Discussion Whereas the biological function of MAM is an important field of research (Rowland and Voeltz, 2012; Kornmann, 2013), their physiological regulation is still largely unknown.”
BackgroundInfluentialFiladi, R., Greotti, E., Turacchio, G., Luini, A., Pozzan, T., & Pizzo, P. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.05.013 · Cited by 173
A Role for the Ancient SNARE Syntaxin 17 in Regulating Mitochondrial Division
Arasaki, K., Shimizu, H., Mogari, H., Nishida, N., Hirota, N., Furuno, A., Kudo, Y., Baba, M., Baba, N., Cheng, J., et al. (2015) · Developmental Cell · doi:10.1016/j.devcel.2014.12.011 · Cited by 173
Mitochondrial dynamics in the central regulation of metabolism
Nasrallah, C. M., & Horváth, T. L. (2014) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2014.160 · Cited by 176
ER–mitochondria signaling in Parkinson’s disease
Gómez‐Suaga, P., Pedro, J. M. B., González‐Polo, R. A., Fuentes, J. M., & Niso‐Santano, M. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0079-3 · Cited by 169
Xian, H., & Liou, Y. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-00657-z · Cited by 177
ER membranes exhibit phase behavior at sites of organelle contact
King, C., Sengupta, P., Seo, A. Y., & Lippincott‐Schwartz, J. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1910854117 · Cited by 169
Daniele, T., Hurbain, I., Vago, R., Casari, G., Raposo, G., Tacchetti, C., & Schiaffino, M. V. (2014) · Current Biology · doi:10.1016/j.cub.2014.01.007 · Cited by 164
“These interorganellar connections accomplish multiple functions, including calcium signaling, control of lipid biosynthesis, mitochondrial division, and coordinated organelle dynamics [8, 9], and aremodulated by the dynamin-like GTPasemitofusin (Mfn) 2, located both onmitochondrial and ERmembranes [10].”
The Interface Between ER and Mitochondria: Molecular Compositions and Functions.
Lee, S., & Min, K. (2018) · Europe PMC (PubMed Central) · doi:10.14348/molcells.2018.0438 · Cited by 160
“buffering and lipid traffic that regulates lipid processing (de Brito and Scorrano, 2010; Hayashi et al., 2009; Rowland and Voeltz, 2012; Vance, 2014).”
BackgroundMehrshahi, P., Stefano, G., Andaloro, J. M., Brandizzí, F., Froehlich, J. E., & DellaPenna, D. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1306331110 · Cited by 160
“Precedent exists for involvement of membrane contact sites in organelle-spanning pathways, because the majority of phosphatidylethanolamine and phosphatidylcholine synthesis in yeast and mammals requires mitochondria:ER contact sites (27, 28), although how these membrane lipids traverse the two organelles remains uncl…”
BackgroundSun, L., Wang, Y., Cen, J., Ma, X., Cui, L., Qiu, Z., Zhang, Z., Li, H., Yang, R., Wang, C., et al. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0359-5 · Cited by 161
Multivesicular body formation enhancement and exosome release during endoplasmic reticulum stress
Kanemoto, S., Nitani, R., Murakami, T., Kaneko, M., Asada, R., Matsuhisa, K., Saito, A., & Imaizumi, K. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.10.019 · Cited by 158
No peroxisome is an island — Peroxisome contact sites
Shai, N., Schuldiner, M., & Zalckvar, E. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.09.016 · Cited by 155
“Indeed, the twomost studied functions of contact sites are the exchange of lipids and Ca (reviewed in [2,4]).”
Background
Metadata
- Authors
- Rowland, A. A., & Voeltz, G. K.
- Affiliations
- University of Colorado Boulder (US)
- Corresponding author
- Voeltz, Gia K.
- ORCID
- Voeltz, Gia K.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2012-09-20
- Volume
- 13
- Issue
- 10
- Pages
- 607-615
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- PMC
- PMC5111635
- OpenAlex
- W2117692658
- Cited by
- 1,018
- References
- 84
- Citations by year
- 2026: 67 · 2025: 81 · 2024: 89 · 2023: 81 · 2022: 81 · 2021: 79 · 2020: 77 · 2019: 68 · 2018: 70 · 2017: 76 · 2016: 67 · 2015: 71 · 2014: 57 · 2013: 51 · 2012: 3
- FWCI
- 5.31
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (GM07135, R01GM083977, T32GM007135)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- endoplasmic reticulum-mitochondria contacts, organelle tethering, lipogenesis, calcium signaling, mitochondrial biogenesis, intracellular trafficking
- MeSH terms
- Animals, Endoplasmic Reticulum, Lipids, Mitochondria, Signal Transduction, Calcium Signaling, Protein Transport, Mitochondrial Membranes, Mitochondrial Turnover
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