The AAA+ ATPase ATAD3A Controls Mitochondrial Dynamics at the Interface of the Inner and Outer Membranes
Open accessAbstract
Dynamic interactions between components of the outer (OM) and inner (IM) membranes control a number of critical mitochondrial functions such as channeling of metabolites and coordinated fission and fusion. We identify here the mitochondrial AAA(+) ATPase protein ATAD3A specific to multicellular eukaryotes as a participant in these interactions. The N-terminal domain interacts with the OM. A central transmembrane segment (TMS) anchors the protein in the IM and positions the C-terminal AAA(+) ATPase domain in the matrix. Invalidation studies in Drosophila and in a human steroidogenic cell line showed that ATAD3A is required for normal cell growth and cholesterol channeling at contact sites. Using dominant-negative mutants, including a defective ATP-binding mutant and a truncated 50-amino-acid N-terminus mutant, we showed that ATAD3A regulates dynamic interactions between the mitochondrial OM and IM sensed by the cell fission machinery. The capacity of ATAD3A to impact essential mitochondrial functions and organization suggests that it possesses unique properties in regulating mitochondrial dynamics and cellular functions in multicellular organisms.
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ATAD3A is characterized by two N-terminal coiled-coil domains, a central transmembrane helix, and a conserved C-terminal AAA+-type ATPase domain.
“ATAD3A is characterized by two N-terminal coiled-coil domains: a central transmembrane helix and a conserved C-terminal AAA+-type ATPase domain (143).”
From Adrenal Mitochondria and Steroidogenesis: From Individual Proteins to Functional Protein Assemblies (2016) · cites this paper as [143]
ATAD3A localizes to mitochondria and appears to be involved in mitochondrial membrane dynamics.
“Several studies have localized ATAD3A to the mitochondria (143, 144), where is appears to be involved in mitochondrial membrane dynamics.”
From Adrenal Mitochondria and Steroidogenesis: From Individual Proteins to Functional Protein Assemblies (2016) · cites this paper as [143]
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- Authors
- Gilquin, B., Taillebourg, E., Cherradi, N., Hubstenberger, A., Gay, O., Merle, N., Assard, N., Fauvarque, M.-O., Tomohiro, S., Kuge, O., & Baudier, J.
- Affiliations
- Inserm (FR)
- Kyushu University (JP)
- ORCID
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2010-04-01
- Volume
- 30
- Issue
- 8
- Pages
- 1984-1996
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC2849464
- OpenAlex
- W2133572194
- Cited by
- 171
- References
- 2
- Citations by year
- 2026: 10 · 2025: 15 · 2024: 14 · 2023: 23 · 2022: 14 · 2021: 13 · 2020: 13 · 2019: 10 · 2018: 5 · 2017: 8 · 2016: 7 · 2015: 4 · 2014: 11 · 2013: 7 · 2012: 11
- FWCI
- 3.13
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular and Cellular Biology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- 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 › ATP Synthase and ATPases Research
- Keywords
- ATAD3A, AAA+ ATPase, mitochondrial dynamics, mitochondrial fission, mitochondrial fusion, mitochondrial outer membrane, inner mitochondrial membrane, mitochondrial contact sites, transmembrane helices, ATP-binding domain, Drosophila, steroidogenic cells, cell growth
- MeSH terms
- ATPases Associated with Diverse Cellular Activities, Adenosine Triphosphatases, Adenosine Triphosphate, Amino Acid Sequence, Animals, Cell Line, DNA-Binding Proteins, Drosophila melanogaster, Humans, Membrane Proteins, Mitochondria, Molecular Sequence Data, Sequence Alignment, Protein Structure, Tertiary, Two-Hybrid System Techniques, Mitochondrial Proteins, Drosophila Proteins, Mitochondrial Membranes
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