ArticleCell structure and function2024
Possible roles of CAHS proteins from Tardigrade in osmotic stress tolerance in mammalian cells.
Article in Cell structure and function, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- 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
- Cytoplasmic abundant heat-soluble proteins from tardigrades protect synthetic cells under stress.Nature communications · 2026Article
- Tardigrades' cytoplasmic abundant heat soluble proteins serve as membrane protectors during dehydration.Research square · 2025Article
- A phase transition modulates the protective function of a tardigrade disordered protein during desiccation.Protein science : a publication of the Protein Society · 2025Article
- Possible roles of CAHS proteins from Tardigrade in osmotic stress tolerance in mammalian cells.Cell structure and function · 2024Article
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5 authors.
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Abstract
Anhydrobiosis, a phenomenon in which organisms survive extreme dehydration by entering a reversible ametabolic state, is a remarkable example of survival strategies. This study focuses on anhydrobiosis in tardigrades, which are known for their resilience to severe environmental conditions. Tardigrades utilize several protective mechanisms against desiccation, notably the constitutive expression of cytoplasmic abundant heat soluble (CAHS) proteins in Ramazzottius varieornatus. These proteins share similarities in their amphiphatic alpha helices with late embryogenesis abundant (LEA) proteins, but differ significantly in their amino acid sequences. In this study, we further explored the functionality of CAHS proteins by analyzing their role in aggregation and tolerance to hyperosmotic stress in mammalian cells. Using live cell imaging, we examined the subcellular localization of several CAHS and LEA proteins in response to hyperosmotic stress. The expression of CAHS1, CAHS3, and CAHS8 tended to enhance the resilience to the hyperosmotic conditions. These findings not only deepen our understanding of the molecular mechanisms of anhydrobiosis but also highlight the potential of CAHS proteins as cryoprotectants.Key words: anhydrobiosis, Tardigrades, live imaging, disordered proteins, desiccation tolerance.
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