The DOI matches its Crossref record; 28 of the 31 references it cites were found in a registry or an index.
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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Cites
Cell-free translation reconstituted with purified components
Shimizu, Y., Inoue, A., Tomari, Y., Suzuki, T., Yokogawa, T., Nishikawa, K., & Ueda, T. (2001) · Nature Biotechnology · doi:10.1038/90802 · Cited by 1,826
Deshaies, R., Koch, B., Werner-Washburne, M., Craig, E., & Schekman, R. (1988) · Nature · doi:10.1038/332800a0 · Cited by 1,368
Common Principles of Protein Translocation Across Membranes
Schatz, G., & Dobberstein, B. (1996) · Science · doi:10.1126/science.271.5255.1519 · Cited by 1,116
Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70
Young, J. C., Hoogenraad, N. J., & Hartl, F. U. (2003) · Cell · doi:10.1016/s0092-8674(02)01250-3 · Cited by 915
Structural Basis of Presequence Recognition by the Mitochondrial Protein Import Receptor Tom20
Abe, Y., Shodai, T., Muto, T., Mihara, K., Torii, H., Nishikawa, S., Endo, T., & Kohda, D. (2000) · Cell · doi:10.1016/s0092-8674(00)80691-1 · Cited by 596
Self-citationVersatility of the mitochondrial protein import machinery
Pfanner, N., & Geissler, A. (2001) · Nature reviews. Molecular cell biology · doi:10.1038/35073006 · Cited by 521
New developments in mitochondrial assembly.
Koehler, C. (2004) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.20.010403.105057 · Cited by 307
Brix, J., Rüdiger, S., Bukau, B., Schneider-Mergener, J., & Pfanner, N. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.23.16522 · Cited by 266
Protein import into yeast mitochondria is accelerated by the outer membrane protein MAS70.
Hines, V., Brandt, A., Griffiths, G., Horstmann, H., Brütsch, H., & Schatz, G. (1990) · EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07517.x · Cited by 246
Multiple pathways for mitochondrial protein traffic
Endo, T., & Yamano, K. (2009) · Biological chemistry · doi:10.1515/bc.2009.087 · Cited by 192
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Items 101–107 of 107
Orchestrating mitochondrial protein import: The emerging role of DYRK1A in health and disease
Shankar, S., & Meisinger, C. (2026) · Protein Science · doi:10.1002/pro.70631
The role of the nucleus in the control of mitochondrial precursor proteins in yeast
Ritzenhofen, K., Rossi, S., Mogk, A., & den Brave, F. (2026) · Protein Science · doi:10.1002/pro.70622
From the cytosol to the inner membrane: biogenesis of the mitochondrial carrier family
Palmer, C. S., Leeming, P. J., & Stojanovski, D. (2026) · Protein Science · doi:10.1002/pro.70537
“…proteins, and TOMM70 is the central receptor that functions in the carrier biogenesis pathway, there exists some overlap in the substrate specificity of the two receptors (Backes et al., 2018; Kato et al., 2013; Melin et al., 2015; Raimi et al., 2024; Wagner et al., 2008; Yamamoto et al., 2009).”
Avendaño‐Monsalve, M. C., Ponce‐Rojas, J. C., & Funes, S. (2021) · TIP Revista Especializada en Ciencias Químico-Biológicas · doi:10.22201/fesz.23958723e.2021.370
“Pfanner, 1997; Brix, Rudiger, Bukau, Scheneider-Mergener & Pfanner, 1999; Yamamoto et al., 2009; Yamano et al., 2008).”
Determinism and contingencies shaped the evolution of mitochondrial protein import
Samuel, R., Oeljeklaus, S., Makki, A., Tachezy, J., Warscheid, B., & Schneider, A. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2017774118 · Cited by 13
Tucker, K., & Park, E. (2019) · bioRxiv · doi:10.1101/798371
The novel mitochondrial outer membrane protein Mcp3 follows a unique IMP-dependent import pathway
Sinzel, M. (2017) · doi:10.15496/publikation-20894
“However, the involvement of Tom70 was also shown for other proteins harboring an MTS, mostly hydrophobic precursors with a tendency to aggregate (Yamamoto et al., 2009).”
Background
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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