The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
Control of mitochondrial morphology by a human mitofusin
Abstract
Although changes in mitochondrial size and arrangement accompany both cellular differentiation and human disease, the mechanisms that mediate mitochondrial fusion, fission and morphogenesis in mammalian cells are not understood. We have identified two human genes encoding potential mediators of mitochondrial fusion. The mitofusins (Mfn1 and Mfn2) are homologs of the Drosophila protein fuzzy onion (Fzo) that associate with mitochondria and alter mitochondrial morphology when expressed by transient transfection in tissue culture cells. An internal region including a predicted bipartite transmembrane domain (TM) is sufficient to target Mfn2 to mitochondria and requires hydrophobic residues within the TM. Co-expression of Mfn2 with a dominant interfering mutant dynamin-related protein (Drp1K38A) proposed to block mitochondrial fission resulted in long mitochondrial filaments and networks. Formation of mitochondrial filaments and networks required a wild-type Mfn2 GTPase domain, suggesting that the Mfn2 GTPase regulates or mediates mitochondrial fusion and that mitofusins and dynamin related GTPases play opposing roles in mitochondrial fusion and fission in mammals, as in yeast.
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“Mitofusin-2 (Mfn2) participates in the maintenance of mitochondrial tubules or networks in mammalian cells (23)(24)(25).”
From Expression of Mfn2, the Charcot-Marie-Tooth Neuropathy Type 2A Gene, in Human Skeletal Muscle (2005) · cites this paper as [24]
In the citing paper
“We show that Mfn2 (mitofusin 2), a mitochondrial membrane protein that participates in mitochondrial fusion in mammalian cells, is induced during myogenesis and contributes to the maintenance and operation of the mitochondrial network.”
From Mitofusin-2 Determines Mitochondrial Network Architecture and Mitochondrial Metabolism (2003) · cites this paper as [22]
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Metadata
- Authors
- Santel, A., & Fuller, M. T.
- Affiliations
- Stanford Medicine (US)
- ORCID
- Fuller, Margaret T.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2001-03-01
- Volume
- 114
- Issue
- 5
- Pages
- 867-874
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2144846851
- Cited by
- 1,012
- References
- 33
- Citations by year
- 2026: 14 · 2025: 38 · 2024: 45 · 2023: 50 · 2022: 50 · 2021: 45 · 2020: 68 · 2019: 73 · 2018: 66 · 2017: 52 · 2016: 42 · 2015: 41 · 2014: 39 · 2013: 43 · 2012: 57
- FWCI
- 8.96
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Cell Science (publishedVersion)
- PubMed (publishedVersion)
- HighWire Press Open Archive (submittedVersion)
- Funders
- National Institutes of Health (5r01hd029194-05)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD29194)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- mitofusin 2, mitofusin 1, mitochondrial fusion, mitochondrial fission, mitochondrial morphology, mitochondrial network, mitochondrial targeting, Drp1, dynamin-related GTPase, GTPase domain, mitochondrial morphogenesis
- MeSH terms
- Animals, Cell Line, Fluorescent Antibody Technique, Humans, Mitochondria, Receptors, CXCR4, GTP Phosphohydrolases
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