Evidence map›Paper›PMID 36717706›Full record

ArticleCommunications biology2023

Tardigrade small heat shock proteins can limit desiccation-induced protein aggregation.

Jonathan D Hibshman, Serena Carra, Bob Goldstein

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
19.4field-weighted citation impact, top 1% of its field
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

21 citing papers in PubMed, 32 citations in OpenAlex.

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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

3 authors at 2 institutions in 2 countries.

Jonathan D HibshmanBiology Department, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA. hibsjo01@email.unc.edu.ORCID 0000-0001-7324-9382
Serena CarraDepartment of Biomedical, Metabolic, and Neural Sciences, University of Modena and Reggio Emilia, Modena, Italy.ORCID 0000-0003-0939-0140
Bob GoldsteinBiology Department, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA.
University of North Carolina at Chapel Hill · USUniversity of Modena and Reggio Emilia · IT

Funding

Virology Research Program (Program 4)P30CA016086 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI David Darr · 1985 to 2026
$201.5M
Identification and analysis of novel tardigrade stress response mechanismsF32GM131577 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI HIBSHMAN, JONATHAN · 2019 to 2022
$216k
National Science Foundation (NSF) IOS 2028860NCI NIH HHS P30 CA016086NIGMS NIH HHS F32 GM131577U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) F32GM131577
6 · The paper itself

Abstract

Small heat shock proteins (sHSPs) are chaperones with well-characterized roles in heat stress, but potential roles for sHSPs in desiccation tolerance have not been as thoroughly explored. We identified nine sHSPs from the tardigrade Hypsibius exemplaris, each containing a conserved alpha-crystallin domain flanked by disordered regions. Many of these sHSPs are highly expressed. Multiple tardigrade and human sHSPs could improve desiccation tolerance of E. coli, suggesting that the capacity to contribute to desicco-protection is a conserved property of some sHSPs. Purification and subsequent analysis of two tardigrade sHSPs, HSP21 and HSP24.6, revealed that these proteins can oligomerize in vitro. These proteins limited heat-induced aggregation of the model enzyme citrate synthase. Heterologous expression of HSP24.6 improved bacterial heat shock survival, and the protein significantly reduced heat-induced aggregation of soluble bacterial protein. Thus, HSP24.6 likely chaperones against protein aggregation to promote heat tolerance. Furthermore, HSP21 and HSP24.6 limited desiccation-induced aggregation and loss of function of citrate synthase. This suggests a mechanism by which tardigrade sHSPs promote desiccation tolerance, by limiting desiccation-induced protein aggregation, thereby maintaining proteostasis and supporting survival. These results suggest that sHSPs provide a mechanism of general stress resistance that can also be deployed to support survival during anhydrobiosis.

Indexed as

Heat-Shock Proteins, SmallTardigradaAnimalsCitrate (si)-SynthaseDesiccationEscherichia coliMolecular ChaperonesProtein AggregatesCitrate (si)-SynthaseHeat-Shock Proteins, SmallMolecular ChaperonesProtein Aggregates

Identifiers

PMID36717706
PMCPMC9887055
OpenAlexW4318478294

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

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 Socratic graph.