ArticleeLife2015
A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis.
Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
What it found
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Who cites it
45 citing papers in PubMed, 73 citations in OpenAlex.
- Disorder with consequence: Phosphorylation sites in HSPB5 yield distinct structural outcomes.bioRxiv : the preprint server for biology · 2025Article
- Small heat shock protein HSPB5 uses disorder to bind zinc with high affinity.bioRxiv : the preprint server for biology · 2025Article
- Switchable client specificity in a dual functional chaperone coordinates light-harvesting complex biogenesis.Science advances · 2025Article
- Activation mechanism of small heat shock protein HSPB5 revealed by disease-associated mutants.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Protein-adaptive differential scanning fluorimetry using conformationally responsive dyes.Nature biotechnology · 2025Article
- Dynamic fibrillar assembly of αB-crystallin induced by perturbation of the conserved NT-IXI motif resolved by cryo-EM.Nature communications · 2024Article
- Article
- Plasma alpha B crystallin as potential biomarker for predicting pre-operative seizures in glioma.BMC neurology · 2024Article
- Dynamic fibrillar assembly of αB-crystallin induced by perturbation of the conserved NT-IXI motif resolved by cryo-EM.bioRxiv : the preprint server for biology · 2024Article
- Therapeutic Applications of Oxysterols and Derivatives in Age-Related Diseases, Infectious and Inflammatory Diseases, and Cancers.Advances in experimental medicine and biology · 2024Review
- HspB5 Chaperone Structure and Activity Are Modulated by Chemical-Scale Interactions in the ACD Dimer Interface.International journal of molecular sciences · 2023Article
- Role of methylation-related genesAnnals of translational medicine · 2022Article
- Twin-arginine translocase component TatB performs folding quality control via a chaperone-like activity.Scientific reports · 2022Article
- Network Pharmacology-Based Strategy to Reveal the Mechanism of Cassiae Semen against Cataracts.Computational and mathematical methods in medicine · 2022Article
- The role ofFrontiers in surgery · 2022Article
- The engineered expression of secreted HSPB5-Fc in CHO cells exhibits cytoprotection in vitro.BMC biotechnology · 2021Article
- α-Crystallins in the Vertebrate Eye Lens: Complex Oligomers and Molecular Chaperones.Annual review of physical chemistry · 2021Review
- CRYAB predicts clinical prognosis and is associated with immunocyte infiltration in colorectal cancer.PeerJ · 2021Article
- Regulation of chaperone function by coupled folding and oligomerization.Science advances · 2020Article
- The multifaceted nature of αB-crystallin.Cell stress & chaperones · 2020Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Small heat shock proteins (sHSPs) are essential 'holdase' chaperones that form large assemblies and respond dynamically to pH and temperature stresses to protect client proteins from aggregation. While the alpha-crystallin domain (ACD) dimer of sHSPs is the universal building block, how the ACD transmits structural changes in response to stress to promote holdase activity is unknown. We found that the dimer interface of HSPB5 is destabilized over physiological pHs and a conserved histidine (His-104) controls interface stability and oligomer structure in response to acidosis. Destabilization by pH or His-104 mutation shifts the ACD from dimer to monomer but also results in a large expansion of HSPB5 oligomer states. Remarkably, His-104 mutant-destabilized oligomers are efficient holdases that reorganize into structurally distinct client-bound complexes. Our data support a model for sHSP function wherein cell stress triggers small perturbations that alter the ACD building blocks to unleash a cryptic mode of chaperone action.
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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.