ArticlePhilosophical transactions of the Royal Society of London. Series B, Biological sciences2013
C-terminal interactions mediate the quaternary dynamics of αB-crystallin.
Article in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 74 citations in OpenAlex.
- Impact of N-terminal domain on the sHSP Lo18 function.Scientific reports · 2025Article
- Filamin C dimerisation is regulated by HSPB7.Nature communications · 2025Article
- The major inducible small heat shock protein HSP20-3 in the tardigrade Ramazzottius varieornatus forms filament-like structures and is an active chaperone.Cell stress & chaperones · 2024Article
- Eye lens β-crystallins are predicted by native ion mobility-mass spectrometry and computations to form compact higher-ordered heterooligomers.Structure (London, England : 1993) · 2023Article
- Is the lipochaperone activity of sHSP a key to the stress response encoded in its primary sequence?Cell stress & chaperones · 2023Review
- Approaches to Heterogeneity in Native Mass Spectrometry.Chemical reviews · 2022Review
- Quaternary Structure and Hetero-Oligomerization of Recombinant Human Small Heat Shock Protein HspB7 (cvHsp).International journal of molecular sciences · 2021Article
- 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
- Article
- Proteostasis is adaptive: Balancing chaperone holdases against foldases.PLoS computational biology · 2020Article
- A novel dominant mutation in CRYAB gene leading to a severe phenotype with childhood onset.Molecular genetics & genomic medicine · 2020Article
- Proteinaceous Transformers: Structural and Functional Variability of Human sHsps.International journal of molecular sciences · 2020Review
- Structural aspects of the human small heat shock proteins related to their functional activities.Cell stress & chaperones · 2020Review
- Structural and functional consequences of age-related isomerization in α-crystallins.The Journal of biological chemistry · 2019Article
- Small heat shock proteins: Simplicity meets complexity.The Journal of biological chemistry · 2019Review
- Mechanistic insights into the switch of αB-crystallin chaperone activity and self-multimerization.The Journal of biological chemistry · 2018Article
- Terminal Regions Confer Plasticity to the Tetrameric Assembly of Human HspB2 and HspB3.Journal of molecular biology · 2018Article
- The influence of the N-terminal region proximal to the core domain on the assembly and chaperone activity of αB-crystallin.Cell stress & chaperones · 2018Article
- Cooperative Assembly of Hsp70 Subdomain Clusters.Biochemistry · 2018Article
- Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions.Science (New York, N.Y.) · 2018Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
αB-crystallin is a highly dynamic, polydisperse small heat-shock protein that can form oligomers ranging in mass from 200 to 800 kDa. Here we use a multifaceted mass spectrometry approach to assess the role of the C-terminal tail in the self-assembly of αB-crystallin. Titration experiments allow us to monitor the binding of peptides representing the C-terminus to the αB-crystallin core domain, and observe individual affinities to both monomeric and dimeric forms. Notably, we find that binding the second peptide equivalent to the core domain dimer is considerably more difficult than the first, suggesting a role of the C-terminus in regulating assembly. This finding motivates us to examine the effect of point mutations in the C-terminus in the full-length protein, by quantifying the changes in oligomeric distribution and corresponding subunit exchange rates. Our results combine to demonstrate that alterations in the C-terminal tail have a significant impact on the thermodynamics and kinetics of αB-crystallin. Remarkably, we find that there is energy compensation between the inter- and intra-dimer interfaces: when one interaction is weakened, the other is strengthened. This allosteric communication between binding sites on αB-crystallin is likely important for its role in binding target proteins.
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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.