The DOI matches its Crossref record; 84 of the 84 references it cites were found in a registry or an index.
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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In the citing paper
“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
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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
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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