ArticleThe Journal of cell biology2022
The cytoprotective sequestration activity of small heat shock proteins is evolutionarily conserved.
Article in The Journal of cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Caenorhabditis elegans small heat-shock protein HSP-12.6 has a highly specialized protective function towards muscle thick filaments in vivo.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Article
- Intermolecular disulfide bond formation promotes Hsp42 higher-order assembly and shapes client selection in yeast.bioRxiv : the preprint server for biology · 2026Article
- Integrative Transcriptome and Metabolome Analysis Reveals the Regulatory Mechanism Underlying the Potential Antioxidant Activity of Neohesperidin Dihydrochalcone-L-Arginine Complex inFoods (Basel, Switzerland) · 2026Article
- Yeast Chronological Lifespan Model as a Tool for Screening Aging Interventions.International journal of molecular sciences · 2026Review
- Dynamics of DNA damage-induced nuclear inclusions are regulated by SUMOylation of Btn2.Nature communications · 2024Article
- TheeLife · 2024Article
- Cytoplasmic redox imbalance in the thioredoxin system activates Hsf1 and results in hyperaccumulation of the sequestrase Hsp42 with misfolded proteins.Molecular biology of the cell · 2024Article
- Chaperone regulation of biomolecular condensates.Frontiers in biophysics · 2024Article
- The beauty and complexity of the small heat shock proteins: a report on the proceedings of the fourth workshop on small heat shock proteins.Cell stress & chaperones · 2023Review
- Tardigrade small heat shock proteins can limit desiccation-induced protein aggregation.Communications biology · 2023Article
- Balanced activities of Hsp70 and the ubiquitin proteasome system underlie cellular protein homeostasis.Frontiers in molecular biosciences · 2022Article
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10 authors.
Funding
Abstract
The chaperone-mediated sequestration of misfolded proteins into inclusions is a pivotal cellular strategy to maintain proteostasis in Saccharomyces cerevisiae, executed by small heat shock proteins (sHsps) Hsp42 and Btn2. Direct homologs of Hsp42 and Btn2 are absent in other organisms, questioning whether sequestration represents a conserved proteostasis strategy and, if so, which factors are involved. We examined sHsps from Escherchia coli, Caenorhabditis elegans, and humans for their ability to complement the defects of yeast sequestrase mutants. We show that sequestration of misfolded proteins is an original and widespread activity among sHsps executed by specific family members. Sequestrase positive C. elegans' sHsps harbor specific sequence features, including a high content of aromatic and methionine residues in disordered N-terminal extensions. Those sHsps buffer limitations in Hsp70 capacity in C. elegans WT animals and are upregulated in long-lived daf-2 mutants, contributing to lifespan extension. Cellular protection by sequestration of misfolded proteins is, therefore, an evolutionarily conserved activity of the sHsp family.
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