ArticleCell stress & chaperones2017
pH-dependent structural modulation is conserved in the human small heat shock protein HSBP1.
Article in Cell stress & chaperones, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 28 citations in OpenAlex.
- Switchable client specificity in a dual functional chaperone coordinates light-harvesting complex biogenesis.Science advances · 2025Article
- Single-molecule observations of human small heat shock proteins in complex with aggregation-prone client proteins.The Biochemical journal · 2025Article
- HspB5 Chaperone Structure and Activity Are Modulated by Chemical-Scale Interactions in the ACD Dimer Interface.International journal of molecular sciences · 2023Article
- A weakened interface in the P182L variant of HSP27 associated with severe Charcot-Marie-Tooth neuropathy causes aberrant binding to interacting proteins.The EMBO journal · 2021Article
- Proteinaceous Transformers: Structural and Functional Variability of Human sHsps.International journal of molecular sciences · 2020Review
- N- and C-terminal regions of αB-crystallin and Hsp27 mediate inhibition of amyloid nucleation, fibril binding, and fibril disaggregation.The Journal of biological chemistry · 2020Article
- Mutations in HspB1 and hereditary neuropathies.Cell stress & chaperones · 2020Review
- Structural aspects of the human small heat shock proteins related to their functional activities.Cell stress & chaperones · 2020Review
- Conditional Disorder in Small Heat-shock Proteins.Journal of molecular biology · 2020Article
- Neuromuscular Diseases Due to Chaperone Mutations: A Review and Some New Results.International journal of molecular sciences · 2020Review
- Release of a disordered domain enhances HspB1 chaperone activity toward tau.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Mechanisms of Small Heat Shock Proteins.Cold Spring Harbor perspectives in biology · 2019Review
- Quaternary structure of α-amino-β-carboxymuconate-ϵ-semialdehyde decarboxylase (ACMSD) controls its activity.The Journal of biological chemistry · 2019Article
- Local unfolding of the HSP27 monomer regulates chaperone activity.Nature communications · 2019Article
- HSPB5 engages multiple states of a destabilized client to enhance chaperone activity in a stress-dependent manner.The Journal of biological chemistry · 2019Article
- Small Heat Shock Proteins, Big Impact on Protein Aggregation in Neurodegenerative Disease.Frontiers in pharmacology · 2019Review
- Competing protein-protein interactions regulate binding of Hsp27 to its client protein tau.Nature communications · 2018Article
- Transcriptome States Reflect Imaging of Aging States.The journals of gerontology. Series A, Biological sciences and medical sciences · 2018Article
- HspB1 and Hsc70 chaperones engage distinct tau species and have different inhibitory effects on amyloid formation.The Journal of biological chemistry · 2018Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The holdase activity and oligomeric propensity of human small heat shock proteins (sHSPs) are regulated by environmental factors. However, atomic-level details are lacking for the mechanisms by which stressors alter sHSP responses. We previously demonstrated that regulation of HSPB5 is mediated by a single conserved histidine over a physiologically relevant pH range of 6.5-7.5. Here, we demonstrate that HSPB1 responds to pH via a similar mechanism through pH-dependent structural changes that are induced via protonation of the structurally analogous histidine. Results presented here show that acquisition of a positive charge, either by protonation of His124 or its substitution by lysine, reduces the stability of the dimer interface of the α-crystallin domain, increases oligomeric size, and modestly increases chaperone activity. Our results suggest a conserved mechanism of pH-dependent structural regulation among the human sHSPs that possess the conserved histidine, although the functional consequences of the structural modulations vary for different sHSPs.
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