ArticleThe EMBO journal2006
Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor.
Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 138 papers, 1 of them a synthesis that pooled it.
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Who cites it
138 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Guidelines for the nomenclature of the human heat shock proteins.Cell stress & chaperones · 2009Guideline
- Hsp70 diversification and repurposing across the tree of life: Lessons from the evolutionary and mechanistic trajectory of the Hsp70-Hsp110 chaperone system.The FEBS journal · 2026Review
- In silico identification of selective cyclodecapeptide inhibitors targeting Plasmodium falciparum Grp78 chaperone.Journal of computer-aided molecular design · 2026Article
- ATP modulates holdase activity of fungal and human 110-kilodalton heat shock proteins to promote protein folding.Protein science : a publication of the Protein Society · 2026Article
- Multiple origins and functions: evolutionary pathways of HSP70 proteins in viruses.The Journal of general virology · 2026Article
- Intracellular aggregation of the transthyretin protein is limited by Hsp70 chaperones.bioRxiv : the preprint server for biology · 2025Article
- Characterization of a New Hsp110 Inhibitor as a Potential Antifungal.Journal of fungi (Basel, Switzerland) · 2024Article
- Early steps of protein disaggregation by Hsp70 chaperone and class B J-domain proteins are shaped by Hsp110.eLife · 2024Article
- Fungal heat shock proteins: molecular phylogenetic insights into the host takeover.Die Naturwissenschaften · 2024Article
- A first-in-class inhibitor of Hsp110 molecular chaperones of pathogenic fungi.Nature communications · 2023Article
- Hsp70 and Hsp110 Chaperones Promote Early Steps of Proteasome Assembly.Biomolecules · 2022Article
- Clearance of variant Creutzfeldt-Jakob disease prions in vivo by the Hsp70 disaggregase system.Brain : a journal of neurology · 2022Article
- Heat shock proteins: Biological functions, pathological roles, and therapeutic opportunities.MedComm · 2022Review
- Developmental Differences between Anthers of Diploid and Autotetraploid Rice at Meiosis.Plants (Basel, Switzerland) · 2022Article
- The Hsc70 disaggregation machinery removes monomer units directly from α-synuclein fibril ends.Nature communications · 2021Article
- Purification and biochemical characterization of Msi3, an essential Hsp110 molecular chaperone in Candida albicans.Cell stress & chaperones · 2021Article
- The functions and regulation of heat shock proteins; key orchestrators of proteostasis and the heat shock response.Archives of toxicology · 2021Review
- Genome-wide imaging screen uncovers molecular determinants of arsenite-induced protein aggregation and toxicity.Journal of cell science · 2021Article
- Cytosolic protein quality control machinery: Interactions of Hsp70 with a network of co-chaperones and substrates.Experimental biology and medicine (Maywood, N.J.) · 2021Review
- Cryptic genetic variation in a heat shock protein modifies the outcome of a mutation affecting epidermal stem cell development in C. elegans.Nature communications · 2021Article
78 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Hsp110 proteins, exclusively found in the eukaryotic cytosol, have significant sequence homology to the Hsp70 molecular chaperone superfamily. Despite this homology and the cellular abundance of these proteins, the precise functional role has remained undefined. Here, we present the intriguing finding that the yeast homologue, Sse1p, acts as an efficient nucleotide exchange factor (NEF) for both yeast cytosolic Hsp70s, Ssa1p and Ssb1p. The mechanism involves formation of a stable nucleotide-sensitive complex, but does not require ATP hydrolysis by Sse1p. The NEF activity of Sse1p stimulates in vitro Ssa1p-mediated refolding of thermally denatured luciferase, and appears to have an essential role in vivo. Overexpression of the only other described cytosolic NEF, Fes1p, can partially compensate for a lethal sse1,2Delta phenotype, however, the cells are sensitive to stress conditions. Furthermore, in the absence of Sse, the in vivo refolding of thermally denatured model proteins is affected. This is the first report of a nucleotide exchange activity for the Hsp110 class of proteins, and provides a key piece in the puzzle of the cellular chaperone network.
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