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Cited by 145Mitochondrial Function and PathologyAutophagy in Disease and TherapyCell death mechanisms and regulation

Mitoguardin regulates mitochondrial fusion through MitoPLD and is required for neuronal homeostasis.

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Zhang, Yongping, Liu, Xiaoman, Bai, Jian, Tian, Xuejun, Zhao, Xiaocui, Liu, Wei, Duan, Xiuying, Shang, Weina +2 more·2016·Molecular Cell
DOI 10.1016/j.molcel.2015.11.017
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Abstract

Mitochondria undergo frequent morphological changes through fission and fusion. Mutations in core members of the mitochondrial fission/fusion machinery are responsible for severe neurodegenerative diseases. However, the mitochondrial fission/fusion mechanisms are poorly understood. We found that the loss of a mitochondrial protein encoding gene, mitoguardin (miga), leads to mitochondrial defects and neurodegeneration in fly eyes. Mammals express two orthologs of miga: Miga1 and Miga2. Both MIGA1 and MIGA2 form homotypic and heterotypic complexes on the outer membrane of the mitochondria. Loss of MIGA results in fragmented mitochondria, whereas overexpression of MIGA leads to clustering and fusion of mitochondria in both fly and mammalian cells. MIGA proteins function downstream of mitofusin and interact with MitoPLD to stabilize MitoPLD and facilitate MitoPLD dimer formation. Therefore, we propose that MIGA proteins promote mitochondrial fusion by regulating mitochondrial phospholipid metabolism via MitoPLD.

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  • Mitochondria with an aspect ratio >2 are considered long mitochondria.

    “Mitochondria with a ratio of >2 were considered as long mitochondria (long-mito), as previously described (Zhang et al., 2016; Wen et al., 2022).”

    From Aging promotes an increase in mitochondrial fragmentation in astrocytes (2024) · cites this paper as Zhang et al., 2016

    The Results describe mitochondria as elongated, and the Introduction discusses elongated mitochondrial networks, but neither gives an aspect-ratio cutoff. Searches for “aspect ratio” and a long-versus-short threshold of 2 found no passage establishing the claimed classification in our copy. (LLM, conf=0.75)

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Cited by

Sorted by citations

Authors
Zhang, Y., Liu, X., Bai, J., Tian, X., Zhao, X., Liu, W., Duan, X., Shang, W., Fan, H.-Y., & Tong, C.
Affiliations
Zhejiang University (CN)
Corresponding author
Tong, Chao
ORCID
Venue
Molecular Cell
Publisher
Elsevier BV
Published
2016-01
Volume
61
Issue
1
Pages
111-124
ISSN
1097-2765 (ISSN-L)
DOI
10.1016/j.molcel.2015.11.017
OpenAlex
W2232974198
Cited by
145
References
9
Citations by year
2026: 16 · 2025: 14 · 2024: 12 · 2023: 19 · 2022: 15 · 2021: 16 · 2020: 15 · 2019: 13 · 2018: 8 · 2017: 12 · 2016: 5
FWCI
3.29
Type
journal article
Language
en
Open access
Licence
Locations
  • Molecular Cell (publishedVersion)
  • PubMed (publishedVersion)
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, phospholipid metabolism, mitofusins, mitochondrial morphology, neurodegeneration, neuronal homeostasis, mitochondrial outer membrane, Drosophila eye, mitochondrial clustering
MeSH terms
Animals, Drosophila melanogaster, Endoribonucleases, Female, Genotype, HeLa Cells, Homeostasis, Humans, Male, Membrane Proteins, Mitochondria, Mutation, Neurons, Phenotype, Phospholipase D, Transfection, Photoreceptor Cells, Invertebrate, Mice, Knockout, Mitochondrial Proteins, Drosophila Proteins, RNA Interference, NIH 3T3 Cells, Mitochondrial Membranes, Mice, Protein Multimerization, HEK293 Cells, Mitochondrial Dynamics

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