Evidence map›Paper›PMID 42069654›Full record

ArticleNature communications2026

Cytoplasmic abundant heat-soluble proteins from tardigrades protect synthetic cells under stress.

Yongkang Xi, Jianming Mao, Samuel J Chen, Hossein Moghimianavval, Young Jin Lee, Ayush Panda, Alexander J Huang, Daniel H Zhou, L Andy Xu, Kayla Y Fu and 3 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors.

Yongkang Xi *Department of Mechanical Engineering, University of Michigan, Ann Arbor, MI, USA.
Jianming Mao *Department of Chemistry, University of Chicago, Chicago, IL, USA.
Samuel J ChenDepartment of Mechanical Engineering, University of Michigan, Ann Arbor, MI, USA.ORCID http://orcid.org/0000-0001-8501-7175
Hossein MoghimianavvalDepartment of Mechanical Engineering, University of Michigan, Ann Arbor, MI, USA.
Young Jin LeeDepartment of Mechanical Engineering, University of Michigan, Ann Arbor, MI, USA.ORCID http://orcid.org/0000-0002-1396-7355
Ayush PandaDepartment of Biophysics, University of Michigan, Ann Arbor, MI, USA.ORCID http://orcid.org/0009-0005-3583-8668
Alexander J HuangDepartment of Mechanical Engineering, University of Michigan, Ann Arbor, MI, USA.
Daniel H ZhouDepartment of Mechanical Engineering, University of Michigan, Ann Arbor, MI, USA.
L Andy XuDepartment of Mechanical Engineering, University of Michigan, Ann Arbor, MI, USA.
Kayla Y FuDepartment of Mechanical Engineering, University of Michigan, Ann Arbor, MI, USA.
Solomon AderaDepartment of Mechanical Engineering, University of Michigan, Ann Arbor, MI, USA.
Andrew L FergusonDepartment of Chemistry, University of Chicago, Chicago, IL, USA. andrewferguson@uchicago.edu.ORCID http://orcid.org/0000-0002-8829-9726
Allen P LiuDepartment of Mechanical Engineering, University of Michigan, Ann Arbor, MI, USA. allenliu@umich.edu.ORCID http://orcid.org/0000-0002-0309-7018

Funding

United States Department of Defense | United States Army | U.S. Army Research, Development and Engineering Command | Army Research Office (ARO) W911NF-23-1-0050United States Department of Defense | United States Army | U.S. Army Research, Development and Engineering Command | Army Research Office (ARO) W911NF-23-1-0084
6 · The paper itself

Abstract

Cytoplasmic abundant heat-soluble (CAHS) proteins, a stress-responsive intrinsically disordered protein from tardigrades, have been discovered to form gel-like networks providing structural support during dehydration, thus enabling anhydrobiosis. However, the mechanism by which CAHS proteins protect the dehydrating cellular membrane remains enigmatic. Using giant unilamellar vesicles (GUVs) as a model membrane system, here we show that encapsulated CAHS12 undergoes a reversible structural transformation that reinforces membrane integrity and preserves encapsulated components, mimicking natural anhydrobiosis. CAHS12-containing GUVs demonstrated stability for weeks and mechanical robustness under dehydration, elevated temperature, and osmotic stresses. Molecular simulations suggest that CAHS12 forms a filamentous network within the vesicle lumen that mitigates membrane collapse and preserves compartmental architecture. Synthetic cells with cell-free transcription-translation capabilities withstand desiccation and recover biochemical activities, akin to the tun state of the tardigrade. This discovery opens up synthetic cell applications in bioengineering, cold-chain-independent biomanufacturing, and adaptive biointerfaces.

Indexed as

Artificial CellsCytoplasmHeat-Shock ProteinsStress, PhysiologicalTardigradaAnimalsCell MembraneDesiccationHot TemperatureOsmotic PressureSolubilityUnilamellar LiposomesHeat-Shock ProteinsUnilamellar Liposomes

Identifiers

PMID42069654
PMCPMC13342215

What OpenQuestion holds

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Registered trials

None linked

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.