Cited by 445Mitochondrial Function and PathologyAutophagy in Disease and TherapyCell death mechanisms and regulation

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Two Mitofusin Proteins, Mammalian Homologues of FZO, with Distinct Functions Are Both Required for Mitochondrial Fusion

Eura, Y.·2003·Journal of Biochemistry

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Abstract

Mitochondria are dynamic organelles that undergo frequent fission and fusion or branching. Although these morphologic changes are considered crucial for cellular functions, the underlying mechanisms remain elusive, especially in mammalian cells. We characterized two rat mitochondrial outer membrane proteins, Mfn1 and Mfn2, with distinct tissue expressions, that are homologous to Drosophila Fzo, a GTPase involved in mitochondrial fusion. Expression of the GTPase-domain mutant of Mfn2 (Mfn2(K109T)) in HeLa cells induced mitochondrial fragmentation in which Mfn2(K109T) localized at the restricted domains. Immuno-electronmicroscopy revealed that Mfn2(K109T) was concentrated at the contact domains between adjacent mitochondria, suggesting that fusion of the outer membrane was arrested at some intermediate step. Mfn1 expression induced highly connected tubular network structures depending on the functional GTPase domain. The Mfn1-induced tubular networks were suppressed by co-expression with Mfn2. In vivo depletion of either isoform by RNA interference revealed that both are required to maintain normal mitochondrial morphology. The fusion of differentially-labeled mitochondria in HeLa cells subjected to depletion of either Mfn isoform and subsequent cell fusion by hemagglutinating virus of Japan revealed that both proteins have distinct functions in mitochondrial fusion. We conclude that the two Mfn isoforms cooperate in mitochondrial fusion in mammalian cells.

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“, N terminal; GTP binding, which is responsible for the binding and hydrolysis of the ATP molecule; medial domain; transmembrane; and two coiled coil domains (CC1 and CC2), which are important for the accurate space orientation of the remaining domains; and the C ter minal domain, which is an effector of GTPase and is…”
Background
The reciprocal regulation between mitochondrial-associated membranes and Notch signaling in skeletal muscle atrophy
Ito, Y., Yamagata, M., Yamamoto, T., Hirasaka, K., Nikawa, T., & Sato, T. (2023) · eLife · doi:10.7554/elife.89381.3 · Cited by 2
Parkin deficiency impairs female fertility, oocyte development, fertilization and mitochondrial function in mice
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“Some key regulators include CLPP, a mitochondrial matrix protease responsible for eliminating misfolded proteins, and the mitofusins MFN1 and MFN2, which mediate outer mitochondrial membrane fusion, a process that supports content exchange and metabolic plasticity 21 – 24 .”
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Background
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Merkwirth, C. (2008) · Kölner Universitäts PublikationsServer (Universität zu Köln)
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Peroxins: A Proliferation Romance amongst Supposition and Disposition
Brocard, C., & Hartig, A. (2007)

Authors: Eura, Y.
Affiliations: Kyushu University (JP)
Corresponding author: Eura, Y.
ORCID: Eura, Y.
Venue: Journal of Biochemistry
Publisher: Oxford University Press (OUP)
Published: 2003-09-01
Volume: 134
Issue: 3
Pages: 333-344
ISSN: 0021-924X (ISSN-L)
DOI: 10.1093/jb/mvg150
OpenAlex: W2001819241
Cited by: 445
References: 0
Citations by year: 2026: 7 · 2025: 25 · 2024: 24 · 2023: 33 · 2022: 28 · 2021: 35 · 2020: 34 · 2019: 27 · 2018: 21 · 2017: 17 · 2016: 19 · 2015: 16 · 2014: 16 · 2013: 26 · 2012: 22
FWCI: 3.54
Type: journal article
Language: en
Open access: closed
Locations: The Journal of Biochemistry (publishedVersion)
PubMed (publishedVersion)
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 1, mitofusin 2, mitochondrial fusion, mitochondrial fission, mitochondrial morphology, mitochondrial outer membrane, GTPase domain, mitochondrial fragmentation, mitochondrial contact sites, HeLa cells, RNAi knockdown, Sendai virus
MeSH terms: Animals, HeLa Cells, Humans, Membrane Fusion, Membrane Proteins, Mitochondria, Morphogenesis, Mutation, Tissue Distribution, Transfection, Protein Isoforms, GTP Phosphohydrolases, Mitochondrial Proteins, Sendai virus, Drosophila Proteins, RNA, Small Interfering, Rats

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Two Mitofusin Proteins, Mammalian Homologues of FZO, with Distinct Functions Are Both Required for Mitochondrial Fusion

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