New functions of mitochondria associated membranes in cellular signaling
Open accessAbstract
In all eukaryotic cells, the endoplasmic reticulum (ER) and the mitochondria establish a tight interplay, which is structurally and functionally modulated through a proteinaceous tether formed at specific subdomains of the ER membrane, designated mitochondria-associated membranes or MAMs. The tethering function of the MAMs allows the regulation of lipid synthesis and rapid transmission of calcium (Ca(2+)) signals between the ER and mitochondria, which is crucial to shape intracellular Ca(2+) signaling and regulate mitochondrial bioenergetics. Research on the molecular characterization and function of MAMs has boomed in the last few years and the list of signaling and structural proteins dynamically associated with the ER-mitochondria contact sites in physiological and pathological conditions, is rapidly increasing along with the realization of an unprecedented complexity underlying the functional role of MAMs. Besides their established role as a signaling hub for Ca(2+) and lipid transfer between ER and mitochondria, MAMs have been recently shown to regulate mitochondrial shape and motility, energy metabolism and redox status and to be central to the modulation of various key processes like ER stress, autophagy and inflammasome signaling. In this review we will discuss some emerging cell-autonomous and cell non-autonomous roles of the MAMs in mammalian cells and their relevance for important human diseases. This article is part of a Special Issue entitled: Calcium signaling in health and disease. Guest Editors: Geert Bultynck, Jacques Haiech, Claus W. Heizmann, Joachim Krebs, and Marc Moreau.
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Direct interactions between mitochondria and the endoplasmic reticulum, particularly at mitochondria-ER-associated membranes, allow direct calcium exchange between the organelles and facilitate lipid synthesis, exchange, and metabolism.
“direct interactions between mitochondria and the endoplasmic reticulum (ER), particularly at mitochondria–ER-associated membranes (MAM), allow direct calcium exchange between the organelles and facilitate lipid synthesis, exchange, and metabolism [45, 46]”
From Neuronal Apolipoprotein E4 Expression Results in Proteome-Wide Alterations and Compromises Bioenergetic Capacity by Disrupting Mitochondrial Function (2019) · cites this paper as [45]
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- Authors
- van Vliet, A. R., Verfaillie, T., & Agostinis, P.
- Affiliations
- KU Leuven (BE)
- Corresponding author
- Agostinis, Patrizia
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2014-10
- Volume
- 1843
- Issue
- 10
- Pages
- 2253-2262
- ISSN
- 0167-4889 (ISSN-L)
- OpenAlex
- W1968365147
- Cited by
- 353
- References
- 14
- Citations by year
- 2026: 9 · 2025: 14 · 2024: 17 · 2023: 26 · 2022: 27 · 2021: 36 · 2020: 33 · 2019: 38 · 2018: 38 · 2017: 37 · 2016: 31 · 2015: 34 · 2014: 13
- FWCI
- 3.63
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (publishedVersion)
- PubMed (publishedVersion)
- Lirias (submittedVersion)
- Funders
- KU Leuven (GOA/11/2009)
- Belgian State, Science Policy Office (IAP6/18)
- IWT Vlaanderen
- 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 › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- mitochondria-associated membranes, ER-mitochondria contact sites, calcium signaling, lipid transfer, mitochondrial bioenergetics, endoplasmic reticulum stress, autophagy, inflammasome signaling, redox regulation, energy metabolism, human disease
- MeSH terms
- Animals, Calcium, Endoplasmic Reticulum, Energy Metabolism, Humans, Mitochondria, Neoplasms, Signal Transduction, Gene Expression, Cell Death, Neurodegenerative Diseases, Calcium Signaling, Mitochondrial Proteins, Mitochondrial Membranes, Endoplasmic Reticulum Stress
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