ReviewCellular and molecular life sciences : CMLS2021
The Hsp70-Hsp90 go-between Hop/Stip1/Sti1 is a proteostatic switch and may be a drug target in cancer and neurodegeneration.
Review in Cellular and molecular life sciences : CMLS, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 63 citations in OpenAlex.
- Coordinated regulation of the metaboproteome by Hsp90 chaperones controls metabolic plasticity.iScience · 2026Article
- Review
- Whole-blood transcriptomic response to whole-body hyperthermia in participants with major depressive disorder.Brain, behavior, & immunity - health · 2026Article
- Ligand-driven modulation of chaperone-cochaperone networks shapes proteostasis outcomes.Protein science : a publication of the Protein Society · 2026Article
- A discovery protein panel for brain predicted age discordance using MRI in neurologically healthy individuals.Frontiers in cell and developmental biology · 2026Article
- Discovery of novel peptidomimetics against HSP90-HOP interactions towards improved cancer therapeutics using machine learning strategies.Frontiers in bioinformatics · 2026Article
- STIP1/HOP promotes the formation of cytotoxic α-synuclein oligomers.Molecular neurodegeneration advances · 2026Article
- Unraveling the mechanism of tetracycline-induced renal injury: an evaluation of drug safety based on network toxicology and molecular dynamics simulations.BMC pharmacology & toxicology · 2025Article
- STIP1 drives Metabolic Reprogramming in Esophageal Squamous Cell Carcinoma via AHCY-LDHA Axis.Exploration (Beijing, China) · 2025Article
- Stress-inducible phosphoprotein 1 (STIP1) is a critical stemness regulator in mouse embryonic stem cells and early mammalian development.Communications biology · 2025Article
- Reduced fungal protein acetylation mediates the antimicrobial activity of a rhizosphere bacterium against a phytopathogenic fungus.Nature communications · 2025Article
- Regulation of physiological and pathological condensates by molecular chaperones.The FEBS journal · 2025Review
- Stress-inducible phosphoprotein 1 (Sti1/Stip1/Hop) sequesters misfolded proteins during stress.The FEBS journal · 2025Article
- The causal effects of 2,821 protein level ratios on non-small cell lung cancer: a two-sample Mendelian randomization study.Translational cancer research · 2025Article
- Chaperone-dependent and chaperone-independent functions of carboxylate clamp tetratricopeptide repeat (CC-TPR) proteins.Trends in biochemical sciences · 2025Review
- Heat shock protein 70 enhances viral replication by stabilizing Senecavirus A nonstructural proteins L and 3D.Veterinary research · 2024Article
- Decreased Hsp90 activity protects against TDP-43 neurotoxicity in a C. elegans model of amyotrophic lateral sclerosis.PLoS genetics · 2024Article
- The J Domain Proteins ofInternational journal of molecular sciences · 2024Review
- Modulators of the Hop-HSP90 Protein-Protein Interaction Disrupt KSHV Lytic Replication.ACS infectious diseases · 2024Article
- Kinesin-1 mediates proper ER folding of the CaEMBO reports · 2024Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Hsp70 and Hsp90 molecular chaperone systems are critical regulators of protein homeostasis (proteostasis) in eukaryotes under normal and stressed conditions. The Hsp70 and Hsp90 systems physically and functionally interact to ensure cellular proteostasis. Co-chaperones interact with Hsp70 and Hsp90 to regulate and to promote their molecular chaperone functions. Mammalian Hop, also called Stip1, and its budding yeast ortholog Sti1 are eukaryote-specific co-chaperones, which have been thought to be essential for substrate ("client") transfer from Hsp70 to Hsp90. Substrate transfer is facilitated by the ability of Hop to interact simultaneously with Hsp70 and Hsp90 as part of a ternary complex. Intriguingly, in prokaryotes, which lack a Hop ortholog, the Hsp70 and Hsp90 orthologs interact directly. Recent evidence shows that eukaryotic Hsp70 and Hsp90 can also form a prokaryote-like binary chaperone complex in the absence of Hop, and that this binary complex displays enhanced protein folding and anti-aggregation activities. The canonical Hsp70-Hop-Hsp90 ternary chaperone complex is essential for optimal maturation and stability of a small subset of clients, including the glucocorticoid receptor, the tyrosine kinase v-Src, and the 26S/30S proteasome. Whereas many cancers have increased levels of Hop, the levels of Hop decrease in the aging human brain. Since Hop is not essential in all eukaryotic cells and organisms, tuning Hop levels or activity might be beneficial for the treatment of cancer and neurodegeneration.
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