Mitochondrial Fusion and Fission in Mammals

Chan, David C.

doi:10.1146/annurev.cellbio.22.010305.104638

Cited by 972Mitochondrial Function and PathologyAutophagy in Disease and TherapyCell death mechanisms and regulation

Mitochondrial Fusion and Fission in Mammals

Chan, David C.·2006·Annual Review of Cell and Developmental Biology

DOI 10.1146/annurev.cellbio.22.010305.104638

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Abstract

Eukaryotic cells maintain the overall shape of their mitochondria by balancing the opposing processes of mitochondrial fusion and fission. Unbalanced fission leads to mitochondrial fragmentation, and unbalanced fusion leads to mitochondrial elongation. Moreover, these processes control not only the shape but also the function of mitochondria. Mitochondrial dynamics allows mitochondria to interact with each other; without such dynamics, the mitochondrial population consists of autonomous organelles that have impaired function. Key components of the mitochondrial fusion and fission machinery have been identified, allowing initial dissection of their mechanisms of action. These components play important roles in mitochondrial function and development as well as programmed cell death. Disruption of the fusion machinery leads to neurodegenerative disease.

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“Conceivably, endosymbiosis would put a high premium on the evolution of the cytoskeleton that is intimately involved, among other processes, in mitochondrial dynamics [137,138].”
From The origins of phagocytosis and eukaryogenesis (2009) · cites this paper as [137]
The frequencies of fusion and fission events are balanced to maintain the overall morphology of the mitochondrial population.
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From Mitochondrial Fission Contributes to Mitochondrial Dysfunction and Insulin Resistance in Skeletal Muscle (2012) · cites this paper as [8]
Mitochondrial fusion and fission are regulated by Mfn1&2, OPA1, DRP1, and FIS1 proteins.
“Indeed, mitochondria form a dynamic network, with the ability to undergo fusion and fission events, processes collectively known as mitochondrial dynamics (Chan, 2006), which are regulated by Mitofusins 1 & 2 (Mfn 1 & 2) and OPtic Atrophy 1 (OPA-1) and Dynamin-Related Protein 1 (DRP1) and mitochondrial-FISsion 1 protein (FIS1) proteins, respectively (Chan, 2006).”
From Effects of Aging and Caloric Restriction on Fiber Type Composition, Mitochondrial Morphology and Dynamics in Rat Oxidative and Glycolytic Muscles (2019) · cites this paper as Chan, 2006
Mitochondria form a dynamic network with the ability to undergo fusion and fission events.
“Indeed, mitochondria form a dynamic network, with the ability to undergo fusion and fission events, processes collectively known as mitochondrial dynamics (Chan, 2006), which are regulated by Mitofusins 1 & 2 (Mfn 1 & 2) and OPtic Atrophy 1 (OPA-1) and Dynamin-Related Protein 1 (DRP1) and mitochondrial-FISsion 1 protein (FIS1) proteins, respectively (Chan, 2006).”
From Effects of Aging and Caloric Restriction on Fiber Type Composition, Mitochondrial Morphology and Dynamics in Rat Oxidative and Glycolytic Muscles (2019) · cites this paper as Chan, 2006
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Peroxisome elongation and constriction but not fission can occur independently of dynamin-like protein 1
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Deficit of in vivo mitochondrial ATP production in OPA1‐related dominant optic atrophy
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Cells lacking Pcp1p/Ugo2p, a rhomboid-like protease required for Mgm1p processing, lose mtDNA and mitochondrial structure in a Dnm1p-dependent manner, but remain competent for mitochondrial fusion
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Fusion of mitochondria in mammalian cells is dependent on the mitochondrial inner membrane potential and independent of microtubules or actin
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Spatial and temporal dynamics of budding yeast mitochondria lacking the division component Fis1p
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Dominant optic atrophy, sensorineural hearing loss, ptosis, and ophthalmoplegia: A syndrome caused by a missense mutation in OPA1
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The WD-repeats of Net2p Interact with Dnm1p and Fis1p to Regulate Division of Mitochondria
Cerveny, K. L., & Jensen, R. E. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-02-0092 · Cited by 103 · see citing works
How mitochondria fuse
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Cytosolic domain of the human mitochondrial fission protein fis1 adopts a TPR fold
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The role of Fis1p–Mdv1p interactions in mitochondrial fission complex assembly
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Expression of the Opa1 Mitochondrial Protein in Retinal Ganglion Cells: Its Downregulation Causes Aggregation of the Mitochondrial Network
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Two Dictyostelium Orthologs of the Prokaryotic Cell Division Protein FtsZ Localize to Mitochondria and Are Required for the Maintenance of Normal Mitochondrial Morphology
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Novel Structure of the N Terminus in Yeast Fis1 Correlates with a Specialized Function in Mitochondrial Fission
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Diverse Eukaryotes have Retained Mitochondrial Homologues of the Bacterial Division Protein FtsZ
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OPA1 expression in the normal rat retina and optic nerve
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OPA1 , the Disease Gene for Autosomal Dominant Optic Atrophy, Is Specifically Expressed in Ganglion Cells and Intrinsic Neurons of the Retina
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Mitochondria: More Than Just a Powerhouse
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Mitofusins and OPA1 mediate sequential steps in mitochondrial membrane fusion
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Self-citation
Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission
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Prolonged cigarette smoke exposure alters mitochondrial structure and function in airway epithelial cells
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Physiological diversity of mitochondrial oxidative phosphorylation
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“Conceivably, endosymbiosis would put a high premium on the evolution of the cytoskeleton that is intimately involved, among other processes, in mitochondrial dynamics [137,138].”
Background
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“network, with the ability to undergo fusion and fission events, processes collectively known as mitochondrial dynamics (Chan, 2006), which are regulated by Mitofusins 1 & 2 (Mfn 1 & 2) and OPtic Atrophy 1 (OPA-1), and Dynamin-Related Protein 1 (DRP1) and mitochondrial-FISsion 1 protein (FIS1) proteins, respectively (C…”
BackgroundInfluential
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Authors: Chan, D. C.
Affiliations: California Institute of Technology (US)
Corresponding author: Chan, David C.
ORCID: Chan, David C.
Venue: Annual Review of Cell and Developmental Biology
Publisher: Annual Reviews
Published: 2006-11-01
Volume: 22
Issue: 1
Pages: 79-99
ISSN: 1081-0706 (ISSN-L)
1530-8995
DOI: 10.1146/annurev.cellbio.22.010305.104638
OpenAlex: W2136937485
Cited by: 972
References: 106
Citations by year: 2026: 14 · 2025: 33 · 2024: 41 · 2023: 43 · 2022: 42 · 2021: 51 · 2020: 65 · 2019: 44 · 2018: 52 · 2017: 54 · 2016: 57 · 2015: 50 · 2014: 59 · 2013: 47 · 2012: 63
FWCI: 3.87
Type: journal article
Language: en
Open access: closed
Locations: Annual Review of Cell and Developmental Biology (publishedVersion)
PubMed (publishedVersion)
CaltechAUTHORS (California Institute of Technology) (submittedVersion)
Funders: Muscular Dystrophy Association
United Mitochondrial Disease Foundation
National Institutes of Health
National Institute of General Medical Sciences (R01GM062967, GM062967)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Keywords: mitochondrial fusion, mitochondrial fission, mitochondrial dynamics, mitochondrial fragmentation, mitochondrial elongation, mitochondrial morphology, mitochondrial function, mitochondrial development, programmed cell death, neurodegenerative diseases, mammalian mitochondria
MeSH terms: Animals, Humans, Mammals, Mitochondria, Mitochondrial Proteins

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Mitochondrial Fusion and Fission in Mammals

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