The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
Open accessAbstract
Juxtaposition between endoplasmic reticulum (ER) and mitochondria is a common structural feature, providing the physical basis for intercommunication during Ca(2+) signalling; yet, the molecular mechanisms controlling this interaction are unknown. Here we show that mitofusin 2, a mitochondrial dynamin-related protein mutated in the inherited motor neuropathy Charcot-Marie-Tooth type IIa, is enriched at the ER-mitochondria interface. Ablation or silencing of mitofusin 2 in mouse embryonic fibroblasts and HeLa cells disrupts ER morphology and loosens ER-mitochondria interactions, thereby reducing the efficiency of mitochondrial Ca(2+) uptake in response to stimuli that generate inositol-1,4,5-trisphosphate. An in vitro assay as well as genetic and biochemical evidences support a model in which mitofusin 2 on the ER bridges the two organelles by engaging in homotypic and heterotypic complexes with mitofusin 1 or 2 on the surface of mitochondria. Thus, mitofusin 2 tethers ER to mitochondria, a juxtaposition required for efficient mitochondrial Ca(2+) uptake.
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In the citing paper
“Other important MAM tethering proteins are B-cell receptor–associated protein 31, mitochondrial fission 1 protein [96], and mitofusin [97].”
From Neuronal Apolipoprotein E4 Expression Results in Proteome-Wide Alterations and Compromises Bioenergetic Capacity by Disrupting Mitochondrial Function (2019) · cites this paper as [97]
In the citing paper
“Marf/Mfn is a mitochondrial fusion protein with pleiotropic functions [39,40] that is also a target of Parkin-dependent ubiquitination upon stress-induced mitophagy.”
From USP8 Down-Regulation Promotes Parkin-Independent Mitophagy in the Drosophila Brain and in Human Neurons (2023) · cites this paper as [39]
In the citing paper
“MFN2, and not MFN1, is expressed on the mitochondria-associated endoplasmic reticulum membranes (MAM) and, to a lesser extent, to the endoplasmic/sarcoplasmic reticulum (ER/SR) [63, 64].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [63]
In the citing paper
“Indeed, MFN2 bridges mitochondria to ER/SR, facilitating critical processes linked to ER–mitochondria interactions like calcium homeostasis and the modulation of the UPR during ER stress via PERK [63, 65–68].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [63]
In the citing paper
“ER stress is induced by the decrease of the ER–mitochondria tethering protein Mfn2 and the down- and upregulation of the ER chaperones calnexin and Bip/Grp78, respectively [63, 65, 66, 213].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [63]
In the citing paper
“Despite some redundancies in their function, the two proteins possess several distinct properties, suggesting that they fulfill different roles in fusion (de Brito and Scorrano, 2008; Eura et al., 2003; Ishihara et al., 2004).”
From New insights into the role of mitochondria in aging: mitochondrial dynamics and more (2010) · cites this paper as de Brito and Scorrano, 2008
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Metadata
- Authors
- de Brito, O. M., & Scorrano, L.
- Affiliations
- University of Geneva (CH)
- Corresponding author
- Scorrano, Luca
- ORCID
- Scorrano, Luca
- Venue
- Nature
- Published
- 2008-12-01
- Volume
- 456
- Issue
- 7222
- Pages
- 605-610
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2166432730
- Cited by
- 2,442
- References
- 35
- Citations by year
- 2026: 105 · 2025: 142 · 2024: 136 · 2023: 142 · 2022: 139 · 2021: 188 · 2020: 186 · 2019: 148 · 2018: 132 · 2017: 175 · 2016: 129 · 2015: 119 · 2014: 132 · 2013: 133 · 2012: 145
- FWCI
- 39.45
- Type
- journal article
- Language
- en
- Update notices
- correction (2014-09-10)
- Open access
- Licence
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- Padua Research Archive (University of Padova) (submittedVersion)
- 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
- mitofusin 2, mitochondrial calcium uptake, inositol 1,4,5-trisphosphate, calcium signaling, dynamin-related proteins, ER morphology, calcium homeostasis
- MeSH terms
- Animals, Calcium, Charcot-Marie-Tooth Disease, Endoplasmic Reticulum, Fibroblasts, HeLa Cells, Humans, Membrane Proteins, Mitochondria, Inositol 1,4,5-Trisphosphate, Calcium Signaling, GTP Phosphohydrolases, Mitochondrial Proteins, Mice, Organelle Shape
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