ArticleProceedings of the National Academy of Sciences of the United States of America2010
Quaternary dynamics and plasticity underlie small heat shock protein chaperone function.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 papers.
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Who cites it
128 citing papers in PubMed, 255 citations in OpenAlex.
- FAIM Inhibits Insulin Amyloidogenesis through a Noncanonical Aggregation Pathway.bioRxiv : the preprint server for biology · 2026Article
- Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026Review
- NMR-guided rational exploration of co-factors in boosting theMagnetic resonance letters · 2025Article
- Single Particle Dynamics of Protein Aggregation and Disaggregation in the Presence of the sHsp Proteins IbpAB.Biochemistry · 2025Article
- Switchable client specificity in a dual functional chaperone coordinates light-harvesting complex biogenesis.Science advances · 2025Article
- Mechanism of small heat shock protein client sequestration and induced polydispersity.Nature communications · 2025Article
- Mass Spectrometry of Proteins and Protein Complexes Electrosprayed in the Presence of Common Biological Buffers Using Theta Emitters.Analytical chemistry · 2025Article
- Small Heat Shock Proteins: Protein Aggregation Amelioration and Neuro- and Age-Protective Roles.International journal of molecular sciences · 2025Review
- The α-crystallin Chaperones Undergo a Quasi-ordered Co-aggregation Process in Response to Saturating Client Interaction.Journal of molecular biology · 2024Article
- Ionizing radiation responses appear incidental to desiccation responses in the bdelloid rotifer Adineta vaga.BMC biology · 2024Article
- Dehydrin CaDHN2 Enhances Drought Tolerance by Affecting Ascorbic Acid Synthesis under Drought in Peppers.Plants (Basel, Switzerland) · 2023Article
- Dissecting the structural heterogeneity of proteins by native mass spectrometry.Protein science : a publication of the Protein Society · 2023Review
- Small heat shock proteins operate as molecular chaperones in the mitochondrial intermembrane space.Nature cell biology · 2023Article
- Tardigrade small heat shock proteins can limit desiccation-induced protein aggregation.Communications biology · 2023Article
- The Common Bean Small Heat Shock Protein Nodulin 22 fromMolecules (Basel, Switzerland) · 2022Article
- Effects of Molecular Crowding and Betaine on HSPB5 Interactions, with Target Proteins Differing in the Quaternary Structure and Aggregation Mechanism.International journal of molecular sciences · 2022Article
- From Small Peptides to Large Proteins against Alzheimer'sDisease.Biomolecules · 2022Review
- ATP-independent molecular chaperone activity generated under reducing conditions.Protein science : a publication of the Protein Society · 2022Article
- Mass Spectrometry Methods for Measuring Protein Stability.Chemical reviews · 2022Review
- Electrospray ionization of native membrane proteins proceedsRSC advances · 2022Article
68 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
Abstract
Small Heat Shock Proteins (sHSPs) are a diverse family of molecular chaperones that prevent protein aggregation by binding clients destabilized during cellular stress. Here we probe the architecture and dynamics of complexes formed between an oligomeric sHSP and client by employing unique mass spectrometry strategies. We observe over 300 different stoichiometries of interaction, demonstrating that an ensemble of structures underlies the protection these chaperones confer to unfolding clients. This astonishing heterogeneity not only makes the system quite distinct in behavior to ATP-dependent chaperones, but also renders it intractable by conventional structural biology approaches. We find that thermally regulated quaternary dynamics of the sHSP establish and maintain the plasticity of the system. This extends the paradigm that intrinsic dynamics are crucial to protein function to include equilibrium fluctuations in quaternary structure, and suggests they are integral to the sHSPs' role in the cellular protein homeostasis network.
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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.