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Roles of Tom70 in Import of Presequence-containing Mitochondrial Proteins
Open accessAbstract
Mitochondrial protein traffic requires precise recognition of the mitochondrial targeting signals by the import receptors on the mitochondrial surface including a general import receptor Tom20 and a receptor for presequence-less proteins, Tom70. Here we took a proteome-wide approach of mitochondrial protein import in vitro to find a set of presequence-containing precursor proteins for recognition by Tom70. The presequences of the Tom70-dependent precursor proteins were recognized by Tom20, whereas their mature parts exhibited Tom70-dependent import when attached to the presequence of Tom70-independent precursor proteins. The mature parts of the Tom70-dependent precursor proteins have the propensity to aggregate, and the presence of the receptor domain of Tom70 prevents their aggregate formation. Therefore Tom70 plays the role of a docking site for not only cytosolic chaperones but also aggregate-prone substrates to maintain their solubility for efficient transfer to downstream components of the mitochondrial import machineries.
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“Indeed, mature protein substrates of Tom70 were observed to be aggregate-prone in the absence of Tom70, suggesting a crucial role of Tom70 in preventing aggregation (69).”
From Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation (2011) · cites this paper as [69]
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“Indeed, mature protein substrates of Tom70 were observed to be aggregate-prone in the absence of Tom70, suggesting a crucial role of Tom70 in preventing aggregation (69).”
From Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation (2011) · cites this paper as [69]
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Cryo-EM structure of the mitochondrial protein-import channel TOM complex at near-atomic resolution
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Metadata
- Authors
- Yamamoto, H., Fukui, K., Takahashi, H., Kitamura, S., Shiota, T., Terao, K., Uchida, M., Esaki, M., Nishikawa, S.-I., Yoshihisa, T., Yamano, K., & Endo, T.
- Affiliations
- Japan Science and Technology Agency (JP)
- Corresponding author
- Endo, Toshiya
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-11
- Volume
- 284
- Issue
- 46
- Pages
- 31635-31646
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2797234
- OpenAlex
- W2050343565
- Cited by
- 119
- References
- 31
- Citations by year
- 2026: 6 · 2025: 8 · 2024: 5 · 2023: 7 · 2022: 8 · 2021: 17 · 2020: 18 · 2019: 6 · 2018: 3 · 2017: 3 · 2016: 7 · 2015: 5 · 2013: 2 · 2012: 5
- FWCI
- 3.22
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Uehara Memorial Foundation
- Japan Society for the Promotion of Science (19058005)
- Japan Science and Technology Agency
- Core Research for Evolutional Science and Technology
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- Tom70, Tom20, mitochondrial protein import, mitochondrial targeting signal, protein aggregation, cytosolic chaperones, precursor protein, mitochondrial import machinery
- MeSH terms
- Mitochondrial Precursor Protein Import Complex Proteins, Mitochondria, Protein Precursors, RNA, Fungal, Saccharomyces cerevisiae, Electrophoresis, Gel, Two-Dimensional, Molecular Chaperones, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Proteome, Mitochondrial Proteins, Saccharomyces cerevisiae Proteins, Mitochondrial Membrane Transport Proteins
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