ArticleThe EMBO journal2005
Maintenance of structure and function of mitochondrial Hsp70 chaperones requires the chaperone Hep1.
Article in The EMBO journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 102 citations in OpenAlex.
- mtHsp70 chaperone converts mitochondrial proteostasis stress into impaired protein import.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- When mitochondria lose their fold: matrix proteostasis and stress signaling.Frontiers in physiology · 2026Review
- Navigating the landscape of protein folding and proteostasis: from molecular chaperones to therapeutic innovations.Signal transduction and targeted therapy · 2025Review
- Molecular regulation of whole genome DNA methylation in heat stress response of dairy cows.BMC genomics · 2025Article
- Two domains of Tim50 coordinate translocation of proteins across the two mitochondrial membranes.Life science alliance · 2023Article
- Human HSP70-escort protein 1 (hHep1) interacts with negatively charged lipid bilayers and cell membranes.Cell stress & chaperones · 2023Article
- Interactions of amyloidogenic proteins with mitochondrial protein import machinery in aging-related neurodegenerative diseases.Frontiers in physiology · 2023Review
- Experimental demonstration and pan-structurome prediction of climate-associated riboSNitches in Arabidopsis.Genome biology · 2022Article
- Comparative analysis of the coordinated motion of Hsp70s from different organelles observed by single-molecule three-color FRET.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Mitochondrial HSP70 Chaperone System-The Influence of Post-Translational Modifications and Involvement in Human Diseases.International journal of molecular sciences · 2021Review
- TheAnnals of translational medicine · 2021Article
- Thermal aggregates of human mortalin and Hsp70-1A behave as supramolecular assemblies.International journal of biological macromolecules · 2020Article
- Biophysical Consequences of EVEN-PLUS Syndrome Mutations for the Function of Mortalin.The journal of physical chemistry. B · 2019Article
- A folding nucleus and minimal ATP binding domain of Hsp70 identified by single-molecule force spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering.Biophysical reviews · 2016Review
- Article
- Mitochondrial heat shock protein (Hsp) 70 and Hsp10 cooperate in the formation of Hsp60 complexes.The Journal of biological chemistry · 2015Article
- Article
- ATP requirement for chloroplast protein import is set by the Km for ATP hydrolysis of stromal Hsp70 in Physcomitrella patens.The Plant cell · 2014Article
- The functional interaction of mitochondrial Hsp70s with the escort protein Zim17 is critical for Fe/S biogenesis and substrate interaction at the inner membrane preprotein translocase.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hsp70 chaperones mediate folding of proteins and prevent their misfolding and aggregation. We report here on a new kind of Hsp70 interacting protein in mitochondria, Hep1. Hep1 is a highly conserved protein present in virtually all eukaryotes. Deletion of HEP1 results in a severe growth defect. Cells lacking Hep1 are deficient in processes that need the function of mitochondrial Hsp70s, such as preprotein import and biogenesis of proteins containing FeS clusters. In the mitochondria of these cells, Hsp70s, Ssc1 and Ssq1 accumulate as insoluble aggregates. We show that it is the nucleotide-free form of mtHsp70 that has a high tendency to self-aggregate. This process is efficiently counteracted by Hep1. We conclude that Hep1 acts as a chaperone that is necessary and sufficient to prevent self-aggregation and to thereby maintain the function of the mitochondrial Hsp70 chaperones.
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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.