ArticleThe EMBO journal2002
The protein import motor of mitochondria: a targeted molecular ratchet driving unfolding and translocation.
Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
30 citing papers in PubMed, 135 citations in OpenAlex.
- Mitochondrial presequences are more than just address labels.Protein science : a publication of the Protein Society · 2026Review
- Molecular machineries and pathways of mitochondrial protein transport.Nature reviews. Molecular cell biology · 2025Review
- Dysfunctional mitochondria trap proteins in the intermembrane space.The EMBO journal · 2025Article
- A protein-specific priority code in presequences determines the efficiency of mitochondrial protein import.PLoS biology · 2025Article
- Protein insertion into the inner membrane of mitochondria: routes and mechanisms.FEBS open bio · 2024Review
- Interactions of amyloidogenic proteins with mitochondrial protein import machinery in aging-related neurodegenerative diseases.Frontiers in physiology · 2023Review
- Whole-cell modeling in yeast predicts compartment-specific proteome constraints that drive metabolic strategies.Nature communications · 2022Article
- Efficient integration of transmembrane domains depends on the folding properties of the upstream sequences.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Transmembrane protein rotaxanes reveal kinetic traps in the refolding of translocated substrates.Communications biology · 2020Article
- Role of the membrane potential in mitochondrial protein unfolding and import.Scientific reports · 2019Article
- Detection of Internal Matrix Targeting Signal-like Sequences (iMTS-Ls) in Mitochondrial Precursor Proteins Using the TargetP Prediction Tool.Bio-protocol · 2018Article
- Tom70 enhances mitochondrial preprotein import efficiency by binding to internal targeting sequences.The Journal of cell biology · 2018Article
- Protein Translocation into the Intermembrane Space and Matrix of Mitochondria: Mechanisms and Driving Forces.Frontiers in molecular biosciences · 2017Review
- Hsp70 chaperones use ATP to remodel native protein oligomers and stable aggregates by entropic pulling.Nature structural & molecular biology · 2016Article
- Functional Diversity of Human Mitochondrial J-proteins Is Independent of Their Association with the Inner Membrane Presequence Translocase.The Journal of biological chemistry · 2016Article
- Role of membrane contact sites in protein import into mitochondria.Protein science : a publication of the Protein Society · 2015Review
- Targeting and assembly of components of the TOC protein import complex at the chloroplast outer envelope membrane.Frontiers in plant science · 2014Review
- Mge1, a nucleotide exchange factor of Hsp70, acts as an oxidative sensor to regulate mitochondrial Hsp70 function.Molecular biology of the cell · 2013Article
- Convergent evolution of heat-inducibility during subfunctionalization of the Hsp70 gene family.BMC evolutionary biology · 2013Article
- A Brownian ratchet for protein translocation including dissociation of ratcheting sites.Journal of mathematical biology · 2013Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Unfolding and import of preproteins into mitochondria are facilitated by a molecular motor in which heat shock protein 70 (Hsp70) in the matrix plays an essential role. Here we present two different experimental approaches to analyze mechanisms underlying this function of Hsp70. First, preproteins containing stretches of glutamic acid (polyE) or glycine (polyG) repeats in front of folded domains were imported into mitochondria. This occurred although Hsp70 cannot pull on these stretches to unfold the folded domains, since it does not bind to polyE and polyG. Secondly, preproteins containing titin immunoglobulin (Ig)-like domains were imported into mitochondria, despite the fact that forces of >200 pN are required to mechanically unfold these domains. Since molecular motors generate forces of approximately 5 pN, Hsp70 could not promote unfolding of the Ig-like domains by mechanical pulling. Our observations suggest that Hsp70 acts as an element of a Brownian ratchet, which mediates unfolding and translocation of preproteins across the mitochondrial membranes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.