Cited by 649Mitochondrial Function and PathologyAutophagy in Disease and TherapyCell death mechanisms and regulation

MiD49 and MiD51, new components of the mitochondrial fission machinery

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Palmer, Catherine S, Osellame, Laura D, Laine, David, Koutsopoulos, Olga S, Frazier, Ann E, Ryan, Michael T·2011·The EMBO Reports

Abstract

Mitochondria form intricate networks through fission and fusion events. Here, we identify mitochondrial dynamics proteins of 49 and 51 kDa (MiD49 and MiD51, respectively) anchored in the mitochondrial outer membrane. MiD49/51 form foci and rings around mitochondria similar to the fission mediator dynamin-related protein 1 (Drp1). MiD49/51 directly recruit Drp1 to the mitochondrial surface, whereas their knockdown reduces Drp1 association, leading to unopposed fusion. Overexpression of MiD49/51 seems to sequester Drp1 from functioning at mitochondria and cause fused tubules to associate with actin. Thus, MiD49/51 are new mediators of mitochondrial division affecting Drp1 action at mitochondria.

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  • MFF, MIEF2/MiD49, and MIEF1/MiD51 bind to DRP1 and arrange assembly of DRP1 oligomers at constriction sites.

    “Instead, it has been reported that other components of the mammalian fission bind to DRP1 and arrange the assembly of DRP1 oligomers at constriction sites: mitochondrial fission factor (MFF), mitochondrial elongation factor 2/mitochondrial dynamics protein 49 (MIEF2/MiD49), and MIEF1/MiD51 [90–93].”

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Authors
Palmer, C. S., Osellame, L. D., Laine, D., Koutsopoulos, O. S., Frazier, A. E., & Ryan, M. T.
Affiliations
La Trobe University (AU)
Corresponding author
Ryan, Michael T
Venue
The EMBO Reports
Published
2011-04-21
Volume
12
Issue
6
Pages
565-573
ISSN
  • 1469-221X (ISSN-L)
  • 1469-3178
OpenAlex
W2005607645
Cited by
649
References
32
Citations by year
2026: 18 · 2025: 34 · 2024: 40 · 2023: 36 · 2022: 48 · 2021: 63 · 2020: 56 · 2019: 47 · 2018: 44 · 2017: 48 · 2016: 45 · 2015: 48 · 2014: 43 · 2013: 45 · 2012: 24
FWCI
15.70
Type
journal article
Language
en
Open access
Locations
  • EMBO Reports (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • UCL Discovery (University College London) (submittedVersion)
Funders
  • Medical Research Council
  • National Health and Medical Research Council
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
MiD51, mitochondrial fission, mitochondrial dynamics, Drp1, mitochondrial outer membrane, mitochondrial fusion, actin, mitochondrial division, dynamin-related proteins
MeSH terms
Actins, Amino Acid Sequence, Animals, Carbonyl Cyanide m-Chlorophenyl Hydrazone, Cell Line, Chlorocebus aethiops, HeLa Cells, Humans, Membrane Proteins, Microtubule-Associated Proteins, Mitochondria, Molecular Sequence Data, Peptide Elongation Factors, Uncoupling Agents, Sequence Alignment, Receptors, Cytoplasmic and Nuclear, COS Cells, Protein Transport, Mitochondrial Proteins, RNA Interference, Mitochondrial Membranes, Mice, Membrane Potential, Mitochondrial

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