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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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BackgroundWorkshop on RanBP2/Nup358 and acute necrotizing encephalopathy
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“MERCS are dynamic structures that remodel in response to intra-and extra cellular signals, affecting the function of both mitochondria and ER [3 – 5].”
Regulation of Endoplasmic Reticulum–Mitochondria Tethering and Ca2+ Fluxes by TDP-43 via GSK3β
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“The most well-characterized organelle contact sites are those between the ER and mitochondria, which have been shown to be involved in the regulation of lipid synthesis, mitochondrial biogenesis and intracellular Ca homeostasis [22].”
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Mutations in unfolded protein response regulator ATF6 cause hearing and vision loss syndrome
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BackgroundShi, R., Liu, Z., Yue, H., Li, M., Liu, S., De, D., Li, R., Chen, Y., Cheng, S., Gu, X., et al. (2024) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-023-00509-x · Cited by 15
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BackgroundEndoplasmic Reticulum–Mitochondria Contacts Are Required for Pexophagy in Saccharomyces cerevisiae
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BackgroundPhysiological functions of mitochondrial Na+-Ca2+ exchanger, NCLX, in lymphocytes
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“Specialized microdomains for the exchange of Ca2+ ions between the two organelles within the contacts sites are also known as mitochondria-associated membranes or MAMs (Rowland and Voeltz 2012; Giorgi et al. 2015; Paillusson et al. 2016).”
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BackgroundMolecular pathways of mitochondrial outer membrane protein degradation
Zheng, J., Li, L., & Jiang, H. (2019) · Biochemical Society Transactions · doi:10.1042/bst20190275 · Cited by 13
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Importance of lipids for upper motor neuron health and disease
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“The ER-mitochondria contact sites are called MAMs (Mitochondria-Associated ER membranes), a major hub for lipid and Ca2+ exchange [161, 162].”
BackgroundLiu, K., Fan, R., & Zhou, Z. (2021) · Poultry Science · doi:10.1016/j.psj.2021.101258 · Cited by 13
“ER is a highly dynamic membrane network and consists of cisternae, linear tubules, and junctions that can be constantly rearranged (Rowland and Voeltz, 2012; Marchi et al., 2014).”
BackgroundPyk2 Regulates MAMs and Mitochondrial Dynamics in Hippocampal Neurons
López-Molina, L., Fernández‐Irigoyen, J., Cifuentes-Díaz, C., Alberch, J., Girault, J., Santamaría, E., Ginés, S., & Giralt, A. (2022) · Cells · doi:10.3390/cells11050842 · Cited by 13
“MAMs regulate not only calcium buffering but also mitochondrial dynamics [17].”
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Chromatin Modifier EP400 Regulates Oocyte Quality and Zygotic Genome Activation in Mice
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Correa, L. O., Jankowski, S. E., Hong, H. S., Armas, N. D., Vijendra, A. I., Reynolds, M. B., Fogo, G. M., Awad, D., Dils, A. T., Inoki, K. A., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114156 · Cited by 14
“75,76 There was no difference in expression of the mitochondrial morphology regulators Drp1 and Opa1 (Figure S6B), 74,77,78 so we investigated MERCS formation.”
BackgroundStrunov, A. A., Boldyreva, L. V., Andreyeva, E. N., Pavlova, G. A., Popova, J. V., Razuvaeva, A. V., Anders, A. F., Renda, F., Pindyurin, A. V., Gatti, M., et al. (2018) · BMC Biology · doi:10.1186/s12915-018-0528-1 · Cited by 13
“However, it is unclear whether the ER and mitochondria also associate during animal cell mitosis [55], although recent work has shown that in dividing HeLa cells, mitochondria tend to localize within the ER folds [56].”
BackgroundLong, M. J. C., Zhao, Y., & Aye, Y. (2020) · RSC Chemical Biology · doi:10.1039/d0cb00041h · Cited by 13
Mohammad, K., Dakik, P., Medkour, Y., McAuley, M., Mitrofanova, D., & Titorenko, V. I. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/3074769 · Cited by 13
Interactions between mitochondria and endoplasmic reticulum in demyelinated axons
Thai, T. Q., Nguyen, H. B., Sui, Y., Ikenaka, K., Oda, T., & Ohno, N. (2018) · Medical Molecular Morphology · doi:10.1007/s00795-018-0212-0 · Cited by 13
Yang, C., Song, G., & Lim, W. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.01.187 · Cited by 13
Ali, M., Rao, K. B. N., Majumder, P., Sarkar, R., & Mapa, K. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.12.003 · Cited by 13
Bruno, S. R., & Anathy, V. (2021) · Histochemistry and Cell Biology · doi:10.1007/s00418-020-01950-1 · Cited by 13
Role of Mitochondria‐Associated ER in Apoptosis
Sang, M., Li, X., Chen, M., Ren, X., Kang, S., Chang, Z., & Wu, Q. (2025) · Cell Biochemistry and Function · doi:10.1002/cbf.70105 · Cited by 12
Mitochondrial dysfunction–induced PANoptosis: Mechanisms, triggers, and disease implications
Pan, L., Fang, S., Kong, F., Ye, S., & Xiong, Y. (2026) · Mitochondrion · doi:10.1016/j.mito.2026.102115 · Cited by 13
Mitochondrial DNA in innate immune responses against infectious diseases
Das, P., & Chakrabarti, O. (2020) · Biochemical Society Transactions · doi:10.1042/bst20200687 · Cited by 12
Zhu, L., Li, B., Chen, D., Chen, N., Xu, L., Zhao, L., & Chen, X. (2022) · Life Sciences · doi:10.1016/j.lfs.2022.120438 · Cited by 12
Anwar, M. O., Islam, M. M., Thakur, V., Kaur, I., & Mohmmed, A. (2022) · Mitochondrion · doi:10.1016/j.mito.2022.05.005 · Cited by 12
Dentoni, G., Naia, L., Portal, B., Leal, N. S., Nilsson, P., Lindskog, M., & Ankarcrona, M. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-220383 · Cited by 13
“To maintain optimal effectiveness and physiological role in the cell, mitochondria need to be in contact with other organelles, specifically the ER at specialized contact sites called MERCS [19].”
Ziegler, D. V., Parashar, K., Leal-Esteban, L. C., López‐Alcalá, J., Castro, W., Zanou, N., Martínez-Carreres, L., Huber, K., Berney, X. P., Malagón, M. M., et al. (2025) · Nature Communications · doi:10.1038/s41467-024-55605-z · Cited by 12
Wang, C., Ji, X., Wang, X., Song, Y., Pan, C., Qian, M., & Jin, Y. (2025) · Environmental Pollution · doi:10.1016/j.envpol.2025.126014 · Cited by 14
Zhang, Y., Xue, Z., Hu, S., Bai, H., Wang, J., & Wang, N. (2021) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.1c02565 · Cited by 12
Badr, H., Blutrich, R., Chan, K., Tong, J., Taylor, P. P., Zhang, W., Kafri, R., Röst, H. L., Tsao, M., & Moran, M. F. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167636 · Cited by 12
Lawal, A. O., Folorunso, I. M., & Iwaloye, O. (2022) · Journal of Diabetes & Metabolic Disorders · doi:10.1007/s40200-022-01057-5 · Cited by 13
“Two-dimensional GC-TOFMS (GC-GC-TOFMS) was employed for analysis under similar circumstances to those previously described [34].”
MethodMitochondria-associated endoplasmic reticulum membranes: A promising toxicity regulation target
Hu, Z., Shi, S., Ou, Y., Hu, F., & Long, D. (2023) · Acta Histochemica · doi:10.1016/j.acthis.2023.152000 · Cited by 12
Curchoe, C. L., & Manor, U. (2017) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.6b00802 · Cited by 12
Yang, Y., Wu, J., Lu, W., Dai, Y., Zhang, Y., & Sun, X. (2023) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.23303 · Cited by 11
Xue, J., Ren, H., Zhang, Q., Gu, J., Xu, Q., Sun, J., Zhang, L., & Zhou, M.-S. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1442831 · Cited by 11
“Structurally, mitochondria and the ER are interconnected through the mitochondrial-associated endoplasmic reticulum membrane, and ER stress is one of the important factors that can induce mitochondrial dysfunction (Rowland and Voeltz, 2012; Wang et al., 2021).”
BackgroundXu, Y., Liu, M., Gao, S., Li, X., Chen, J., & Ye, F. (2024) · NeuroToxicology · doi:10.1016/j.neuro.2024.11.001 · Cited by 12
Chen, Y., Bi, K., Zhang, C., Gu, J., Yu, Z., Lu, J., & Yu, L. (2025) · Hereditas · doi:10.1186/s41065-025-00387-7 · Cited by 11
Endoni, B. T., Koval, O. M., Allamargot, C., Kortlever, T., Qian, L., Sadoski, R. J., Juhr, D., & Grumbach, I. M. (2025) · Cells · doi:10.3390/cells14070482 · Cited by 11
Computational model of polarized actin cables and cytokinetic actin ring formation in budding yeast
Tang, H., Bidone, T. C., & Vavylonis, D. (2015) · Cytoskeleton · doi:10.1002/cm.21258 · Cited by 11
“The cortical ER is associated with actin cytoskeleton [Fehrenbacher et al., 2002] and its inheritance in budding yeast cell is achieved through type V myosin transport on actin cables [Estrada et al., 2003; Du et al., 2004; West et al., 2011; Rowland and Voeltz, 2012].”
BackgroundClusterin is involved in mediating the metabolic function of adipose SIRT1
Zhang, P., Konja, D., Zhang, Y., Xu, A., Lee, I., Jeon, J., Bashiri, G., MITRA, A. K., & Wang, Y. (2021) · iScience · doi:10.1016/j.isci.2021.103709 · Cited by 11
Mitochondria-Endoplasmic Reticulum Interplay Regulates Exo-Cytosis in Human Neuroblastoma Cells
Dentoni, G., Naia, L., & Ankarcrona, M. (2022) · Cells · doi:10.3390/cells11030514 · Cited by 11
“Several physiological functions have been attributed to these structures including Ca2+-shuttling, phospholipid and cholesterol synthesis, bioenergetics, and apoptosis [58].”
BackgroundOligomeric CHMP7 mediates three-way ER junctions and ER-mitochondria interactions
Chu, Q., Wang, J., Du, Y., Zhou, T., Shi, A., Xiong, J., Ji, W.-K., & Deng, L. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01048-2 · Cited by 11
“Importantly, consistent with our imaging results, a small but substantial portion of CHMP7 was enriched in the mitochondrial associated membranes (MAMs) [30] (Fig.”
ResultMitochondria inter-organelle relationships in cancer protein aggregation
Genovese, I., Fornetti, E., & Ruocco, G. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1062993 · Cited by 11
“MAMs have been found highly enriched in these proteins since Ca is essential for mitochondria-dependent energy metabolism, motility, biogenesis, and apoptosis (Giacomello et al., 2007; Baughman et al., 2011; De Stefani et al., 2011; Rowland and Voeltz, 2012; Chaudhuri et al., 2013) (Figure 1A).”
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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