ArticleThe Journal of biological chemistry2010
The 90-kDa heat shock protein Hsp90 protects tubulin against thermal denaturation.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- αB-crystallin elastin-like polypeptides for sustained ocular drug delivery.Drug delivery and translational research · 2026Article
- Proteomic Analysis of Differentially Expressed Plasma Exosome Proteins in Heat-StressedAnimals : an open access journal from MDPI · 2025Article
- Unleash the dogs of death: metacaspase 5, microtubules, and hypersensitive response.Plant cell reports · 2025Article
- β-hydroxybutyrate is a metabolic regulator of proteostasis in the aged and Alzheimer disease brain.Cell chemical biology · 2025Article
- Quantitative proteome analysis of LAP1-deficient human fibroblasts: A pilot approach for predicting the signaling pathways deregulated in LAP1-associated diseases.Biochemistry and biophysics reports · 2024Article
- Capsaicin binds the N-terminus of Hsp90, induces lysosomal degradation of Hsp70, and enhances the anti-tumor effects of 17-AAG (Tanespimycin).Scientific reports · 2023Article
- Actin network architecture can ensure robust centering or sensitive decentering of the centrosome.The EMBO journal · 2022Article
- Targeting HSP90 as a Novel Therapy for Cancer: Mechanistic Insights and Translational Relevance.Cells · 2022Review
- Role of Heat Shock Proteins (HSP70 and HSP90) in Viral Infection.International journal of molecular sciences · 2021Review
- Electrical behaviour and evolutionary computation in thin films of bovine brain microtubules.Scientific reports · 2021Article
- Bioinformatic analysis linking genomic defects to chemosensitivity and mechanism of action.PloS one · 2021Article
- Heat shock response enhanced by cell culture treatment in mouse embryonic stem cell-derived proliferating neural stem cells.PloS one · 2021Article
- Rice Big Grain 1 promotes cell division to enhance organ development, stress tolerance and grain yield.Plant biotechnology journal · 2020Article
- Microtubule Seeded-assembly in the Presence of Poorly Nucleating Nucleotide Analogues.Bio-protocol · 2020Article
- Lattice defects induce microtubule self-renewal.Nature physics · 2019Article
- A CCRK and a MAK Kinase Modulate Cilia Branching and Length via Regulation of Axonemal Microtubule Dynamics in Caenorhabditis elegans.Current biology : CB · 2019Article
- The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease.International journal of molecular sciences · 2018Review
- Dysregulated fibronectin trafficking by Hsp90 inhibition restricts prostate cancer cell invasion.Scientific reports · 2018Article
- Heat Shock Proteins Regulatory Role in Neurodevelopment.Frontiers in neuroscience · 2018Review
- Structural and Functional Recovery of Sensory Cilia in C. elegans IFT Mutants upon Aging.PLoS genetics · 2016Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hsp90 and tubulin are among the most abundant proteins in the cytosol of eukaryotic cells. Although Hsp90 plays key roles in maintaining its client proteins in their active state, tubulin is essential for fundamental processes such as cell morphogenesis and division. Several studies have suggested a possible connection between Hsp90 and the microtubule cytoskeleton. Because tubulin is a labile protein in its soluble form, we investigated whether Hsp90 protects it against thermal denaturation. Both proteins were purified from porcine brain, and their interaction was characterized in vitro by using spectrophotometry, sedimentation assays, video-enhanced differential interference contrast light microscopy, and native polyacrylamide gel electrophoresis. Our results show that Hsp90 protects tubulin against thermal denaturation and keeps it in a state compatible with microtubule polymerization. We demonstrate that Hsp90 cannot resolve tubulin aggregates but that it likely binds early unfolding intermediates, preventing their aggregation. Protection was maximal at a stoichiometry of two molecules of Hsp90 for one of tubulin. This protection does not require ATP binding and hydrolysis by Hsp90, but it is counteracted by geldanamycin, a specific inhibitor of Hsp90.
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