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Cited by 64Heat shock proteins researchMitochondrial Function and PathologyATP Synthase and ATPases Research

Function of Cytosolic Chaperones in Tom70-Mediated Mitochondrial Import

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C.Y. Fan, Anna, C. Young, Jason·2011·Protein & Peptide Letters
DOI 10.2174/092986611794475020PMC PMC5026486
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Abstract

The great majority of mitochondrial proteins are synthesized by cytosolic ribosomes and then imported into the organelle post-translationally. The translocase of the outer membrane (TOM) is a proteinaceous machinery that contains surface receptors for preprotein recognition and also serves as the main entry gateway into mitochondria. Mitochondrial targeting requires various cytosolic factors, in particular the molecular chaperones Hsc70/Hsp70 and Hsp90. The chaperone activity of Hsc70/Hsp70 and Hsp90 occurs in coordinated cycles of ATP hydrolysis and substrate binding, and is regulated by a number of co-chaperone proteins. The import receptor Tom70 is a member of the tetratricopeptide repeat (TPR) co-chaperone family and contains a conserved TPR clamp domain for interaction with Hsc70 and Hsp90. Such interaction is essential for the initiation of the import process. This review will discuss the roles of Hsc70 and Hsp90 in mitochondrial import and summarize recent progress in understanding these pathways. Keywords: Mitochondria, import, chaperone, Tom70, Hsc70, Hsp90, TOM, ATP hydrolysis, TPR, OM, IM, ATP, Saccharomyces cerevisiae, DNA, GIP, TIM, cytosolic, hydrophobic, hexokinases, DnaK, DnaJ, HPD, DNAJA4, NEF, DNA gyrase B, homodimer, OTC, pmAAT, ANT, AAC, PiC, GA, NB, CiC, OGC, TSPO, Tom71, FKBP38, Cdc37Mitochondria, import, chaperone, Tom70, Hsc70, Hsp90, TOM, ATP hydrolysis, TPR, OM, IM, ATP, Saccharomyces cerevisiae, DNA, GIP, TIM, cytosolic, hydrophobic, hexokinases, DnaK, DnaJ, HPD, DNAJA4, NEF, DNA gyrase B, homodimer, OTC, pmAAT, ANT, AAC, PiC, GA, NB, CiC, OGC, TSPO, Tom71, FKBP38, Cdc37

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  • Tom34 is found predominantly in the cytosol and binds Hsp90 and Hsp70, as does Tom70.

    “Although associated with mitochondria, Tom34 is found more predominantly in the cytosol and binds to the chaperone proteins Hsp90 and Hsp70, as does Tom70 (66–68).”

    From Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation (2011) · cites this paper as [68]

    The Tom70 Import Pathway section (page unavailable) says Tom70 interacts with Hsc70/Hsp70 and Hsp90. Our copy does not address Tom34’s localization or its binding to those chaperones (searched: Tom34 and predominantly cytosolic Tom34), so the Tom34 portion is unsupported. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

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Cited by

Sorted by citations

Authors
C.Y. Fan, A., & C. Young, J.
Venue
Protein & Peptide Letters
Publisher
Bentham Science Publishers Ltd.
Published
2011-02-01
Volume
18
Issue
2
Pages
122-131
ISSN
0929-8665 (ISSN-L)
DOI
10.2174/092986611794475020
PMC
PMC5026486
OpenAlex
W1985604548
Cited by
64
References
6
Citations by year
2026: 1 · 2025: 3 · 2024: 2 · 2023: 4 · 2022: 3 · 2021: 4 · 2020: 10 · 2019: 8 · 2018: 8 · 2016: 3 · 2015: 5 · 2014: 2 · 2013: 5 · 2012: 4
FWCI
1.69
Type
journal article
Language
en
Open access
Locations
  • Protein and Peptide Letters (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • Canada Research Chairs
  • U.S. Public Health Service (68825-2, 103329-1)
  • Canadian Institutes of Health Research (68825_2, 103329_1)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
Keywords
mitochondrial protein import, Tom70, Hsc70, HSP90, cytosolic chaperones, TOM complex, ATP hydrolysis, mitochondrial targeting, hydrophobic proteins, Saccharomyces cerevisiae
MeSH terms
Mitochondrial Precursor Protein Import Complex Proteins, Humans, HSP90 Heat-Shock Proteins, Protein Transport, Mitochondrial Membrane Transport Proteins, HSC70 Heat-Shock Proteins

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