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Cited by 1,397Mitochondrial Function and PathologyAutophagy in Disease and TherapyCell death mechanisms and regulation

Mitochondrial dynamics: overview of molecular mechanisms

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Tilokani, Lisa, Nagashima, Shun, Paupe, Vincent, Prudent, Julien·2018·Essays in Biochemistry
DOI 10.1042/ebc20170104PMC PMC6056715
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Abstract

Mitochondria are highly dynamic organelles undergoing coordinated cycles of fission and fusion, referred as ‘mitochondrial dynamics’, in order to maintain their shape, distribution and size. Their transient and rapid morphological adaptations are crucial for many cellular processes such as cell cycle, immunity, apoptosis and mitochondrial quality control. Mutations in the core machinery components and defects in mitochondrial dynamics have been associated with numerous human diseases. These dynamic transitions are mainly ensured by large GTPases belonging to the Dynamin family. Mitochondrial fission is a multi-step process allowing the division of one mitochondrion in two daughter mitochondria. It is regulated by the recruitment of the GTPase Dynamin-related protein 1 (Drp1) by adaptors at actin- and endoplasmic reticulum-mediated mitochondrial constriction sites. Drp1 oligomerization followed by mitochondrial constriction leads to the recruitment of Dynamin 2 to terminate membrane scission. Inner mitochondrial membrane constriction has been proposed to be an independent process regulated by calcium influx. Mitochondrial fusion is driven by a two-step process with the outer mitochondrial membrane fusion mediated by mitofusins 1 and 2 followed by inner membrane fusion, mediated by optic atrophy 1. In addition to the role of membrane lipid composition, several members of the machinery can undergo post-translational modifications modulating these processes. Understanding the molecular mechanisms controlling mitochondrial dynamics is crucial to decipher how mitochondrial shape meets the function and to increase the knowledge on the molecular basis of diseases associated with morphology defects. This article will describe an overview of the molecular mechanisms that govern mitochondrial fission and fusion in mammals.

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  • Mitochondrial dynamics include fusion, fission, and degradation events, linked to mitochondrial function.

    “Mitochondrial dynamics include fusion, fission, and degradation events, linked to mitochondrial function3,4.”

    From Altered mitochondrial dynamics and function in APOE4-expressing astrocytes (2020) · cites this paper as [4]

    The Abstract defines mitochondrial dynamics as coordinated cycles of fission and fusion, and the Introduction links those transitions to mitochondrial function. The section on post-translational modifications says fission can promote degradation of damaged mitochondria, but the paper does not define degradation itself as a mitochondrial dynamics event. Page numbers were not supplied in our copy. (LLM, conf=0.87)

    Experimental — accuracy not yet measured

  • During mitochondrial fission, cytosolic Drp1 is recruited to mitochondrial receptors (e.g., Fis1), allowing mitochondrial partitioning, turnover and reduction of network size under low energetic demand.

    “During mitochondrial fission, cytosolic Drp1 is recruited to mitochondrial receptors (e.g., Fis1)3,4, allowing mitochondrial partitioning, turnover and reduction of network size under low energetic demand4,7.”

    From Altered mitochondrial dynamics and function in APOE4-expressing astrocytes (2020) · cites this paper as [4]

    The “Drp1 and adaptors” section says that mainly cytosolic Drp1 is recruited to mitochondria for fission, and Figure 4 describes division into two daughter mitochondria. But it identifies MFF and MiD49/51—not Fis1—as the relevant Drp1 receptors in mammals under basal conditions. The Introduction links fragmentation to quality control, but the copy does not establish that fission reduces network size specifically under low energetic demand. (LLM, conf=0.87)

    Experimental — accuracy not yet measured

  • Mitochondrial fusion is triggered by increased MMP and involves oligomerization of mitofusins on the OMM.

    “This process is triggered by increased mitochondrial membrane potential (MMP) and involves the oligomerization of mitofusins on the outer mitochondrial membrane (OMM)4.”

    From Altered mitochondrial dynamics and function in APOE4-expressing astrocytes (2020) · cites this paper as [4]

    The ‘Mitofusins and outer mitochondrial membrane fusion’ section (page unavailable) describes mitofusin oligomerization as part of outer-membrane fusion. It does not say that an increase in mitochondrial membrane potential triggers fusion; the passage addressing membrane potential instead describes a drop associated with inner-membrane constriction. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • Several proteins are required for mitochondrial fusion, including the mitofusins (Mfn1/Mfn2).

    “Several proteins are required for mitochondrial fusion, including the mitofusins (Mfn1/Mfn2)3,4.”

    From Altered mitochondrial dynamics and function in APOE4-expressing astrocytes (2020) · cites this paper as [4]

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Authors
Tilokani, L., Nagashima, S., Paupe, V., & Prudent, J.
Affiliations
University of Cambridge (GB)
Corresponding author
Prudent, Julien
ORCID
Venue
Essays in Biochemistry
Publisher
Portland Press Ltd.
Published
2018-07-20
Volume
62
Issue
3
Pages
341-360
ISSN
  • 0071-1365 (ISSN-L)
  • 1744-1358
DOI
10.1042/ebc20170104
PMC
PMC6056715
OpenAlex
W2883221432
Cited by
1,397
References
192
Citations by year
2026: 134 · 2025: 186 · 2024: 244 · 2023: 213 · 2022: 196 · 2021: 181 · 2020: 162 · 2019: 71 · 2018: 8
FWCI
10.30
Type
journal article
Language
en
Open access
Licence
Locations
  • Essays in Biochemistry (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Apollo (University of Cambridge) (submittedVersion, cc-by)
  • Apollo (cc-by)
Funders
  • Daiichi-Sankyo
  • Daiichi Sankyo Foundation of Life Science
  • Medical Research Council (MC_UU_00015/7)
  • Daiichi Sankyo Europe
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 dynamics, mitochondrial fission, mitochondrial fusion, Drp1, dynamin 2, mitofusins, optic atrophy 1, calcium influx, post-translational modification, mitochondrial quality control, mitochondrial morphology, mitochondrial disease
MeSH terms
Animals, Endoplasmic Reticulum, Humans, Mitochondria, Protein Processing, Post-Translational, Mitochondrial Proteins, Mitochondrial Diseases, Mitochondrial Membranes, Mitochondrial Dynamics

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

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