ArticleProtein science : a publication of the Protein Society2024
Labile assembly of a tardigrade protein induces biostasis.
Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 24 citations in OpenAlex.
- Article
- Tardigrade-Derived Strategy for Low-Cost Storage of Cell-Free Expression Lysates.ACS synthetic biology · 2026Article
- Expression of tardigrade extremotolerance-associated proteins improves recovery but not acute stress response of human microvascular endothelial cells.Scientific reports · 2026Article
- Evidence that local viscosity and NOX-dependent ROS increases render the tardigrade H. exemplaris resilient to extreme physical force.bioRxiv : the preprint server for biology · 2026Article
- Chiral inversion mutagenesis identifies geometrically constrained residues within self-associating low-complexity domains.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Cytoplasmic abundant heat-soluble proteins from tardigrades protect synthetic cells under stress.Nature communications · 2026Article
- Disordered but rhythmic-the role of intrinsic protein disorder in eukaryotic circadian timing.FEBS letters · 2026Review
- Fibril Structure of Desiccation-Protective Tardigrade Protein CAHS-8.Angewandte Chemie (International ed. in English) · 2026Article
- Chiral inversion mutagenesis identifies geometrically constrained residues within self-associating low-complexity domains.bioRxiv : the preprint server for biology · 2025Article
- OsmoFold: A high-throughput tool for predicting the impact of osmolytes on protein structure.Biophysical journal · 2025Article
- A phase transition modulates the protective function of a tardigrade disordered protein during desiccation.Protein science : a publication of the Protein Society · 2025Article
- Functional diversity of Arabidopsis late embryogenesis abundant proteins in response to changes in the physicochemical environment.bioRxiv : the preprint server for biology · 2025Article
- Life on the dry side: a roadmap to understanding desiccation tolerance and accelerating translational applications.Nature communications · 2025Review
- Diversity in the protective role(s) of the conserved motif 1 from tardigrade cytoplasmic-abundant heat-soluble proteins during drying.Protein science : a publication of the Protein Society · 2025Article
- Radioprotection redefined: drug discovery at the intersection of tardigrade biology and translational pharmacology.Frontiers in pharmacology · 2025Article
- Disordered proteins interact with the chemical environment to tune their protective function during drying.eLife · 2024Article
- An evaluation of thermal tolerance in six tardigrade species in an active and dry state.Biology open · 2024Article
- Structural adaptability and surface activity of peptides derived from tardigrade proteins.Protein science : a publication of the Protein Society · 2024Article
- Labile assembly of a tardigrade protein induces biostasis.Protein science : a publication of the Protein Society · 2024Article
- Helicity of a tardigrade disordered protein contributes to its protective function during desiccation.Protein science : a publication of the Protein Society · 2024Article
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Authors and funding
25 authors at 8 institutions in 4 countries.
Funding
Abstract
Tardigrades are microscopic animals that survive desiccation by inducing biostasis. To survive drying tardigrades rely on intrinsically disordered CAHS proteins, which also function to prevent perturbations induced by drying in vitro and in heterologous systems. CAHS proteins have been shown to form gels both in vitro and in vivo, which has been speculated to be linked to their protective capacity. However, the sequence features and mechanisms underlying gel formation and the necessity of gelation for protection have not been demonstrated. Here we report a mechanism of fibrillization and gelation for CAHS D similar to that of intermediate filament assembly. We show that in vitro, gelation restricts molecular motion, immobilizing and protecting labile material from the harmful effects of drying. In vivo, we observe that CAHS D forms fibrillar networks during osmotic stress. Fibrillar networking of CAHS D improves survival of osmotically shocked cells. We observe two emergent properties associated with fibrillization; (i) prevention of cell volume change and (ii) reduction of metabolic activity during osmotic shock. We find that there is no significant correlation between maintenance of cell volume and survival, while there is a significant correlation between reduced metabolism and survival. Importantly, CAHS D's fibrillar network formation is reversible and metabolic rates return to control levels after CAHS fibers are resolved. This work provides insights into how tardigrades induce reversible biostasis through the self-assembly of labile CAHS gels.
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