Evidence map›Paper›PMID 34003451›Full record

ArticleCell stress & chaperones2021

Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes.

Paulo R Dores-Silva, David M Cauvi, Amanda L S Coto, Noeli S M Silva, Júlio C Borges, Antonio De Maio

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell stress & chaperones, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

14 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. ame-miR-34 Modulates the Larval Body Weight and Immune Response ofInternational journal of molecular sciences · 2023
    Article
  13. Article
  14. Review
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

6 authors at 3 institutions in 2 countries.

Paulo R Dores-SilvaDepartment of Surgery, School of Medicine, Division of Trauma, Critical Care, Burns and Acute Care Surgery, University of California, San Diego, La Jolla, CA, 92093, USA.
David M CauviDepartment of Surgery, School of Medicine, Division of Trauma, Critical Care, Burns and Acute Care Surgery, University of California, San Diego, La Jolla, CA, 92093, USA.
Amanda L S CotoSão Carlos Institute of Chemistry, University of São Paulo, São Paulo, Brazil.
Noeli S M SilvaSão Carlos Institute of Chemistry, University of São Paulo, São Paulo, Brazil.
Júlio C BorgesSão Carlos Institute of Chemistry, University of São Paulo, São Paulo, Brazil.
Antonio De MaioDepartment of Surgery, School of Medicine, Division of Trauma, Critical Care, Burns and Acute Care Surgery, University of California, San Diego, La Jolla, CA, 92093, USA. ademaio@health.ucsd.edu.ORCID 0000-0002-1520-6381
Universidade de São Paulo · BRUC San Diego Health System · USUniversity of California San Diego · US

Funding

Contribution of Cholesterol Homeostasis for Injury ResolutionR01GM114473 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DE MAIO, ANTONIO · 2015 to 2018
$1.2M
Heat Shock Proteins and the Stress Observation SystemR01GM098455 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DE MAIO, ANTONIO · 2012 to 2015
$1.1M
Conselho Nacional de Pesquisa e Desenvolvimento 303262/2018-4FAPESP 2012/50161-8FAPESP 2014/16646-0FAPESP 2016/22477-1FAPESP 2017/07335-9FAPESP 2017/26131-5NIGMS NIH HHS R01 GM098455NIGMS NIH HHS R01 GM114473
6 · The paper itself

Abstract

Heat shock proteins (HSP) are critical elements for the preservation of cellular homeostasis by participating in an array of biological processes. In addition, HSP play an important role in cellular protection from various environmental stresses. HSP are part of a large family of different molecular mass polypeptides, displaying various expression patterns, subcellular localizations, and diversity functions. An unexpected observation was the detection of HSP on the cell surface. Subsequent studies have demonstrated that HSP have the ability to interact and penetrate lipid bilayers by a process initiated by the recognition of phospholipid heads, followed by conformational changes, membrane insertion, and oligomerization. In the present study, we described the interaction of HSPA8 (HSC70), the constitutive cytosolic member of the HSP70 family, with lipid membranes. HSPA8 showed high selectivity for negatively charged phospholipids, such as phosphatidylserine and cardiolipin, and low affinity for phosphatidylcholine. Membrane insertion was mediated by a spontaneous process driven by increases in entropy and diminished by the presence of ADP or ATP. Finally, HSPA8 was capable of driving into the lipid bilayer HSP90 that does not display any lipid biding capacity by itself. This observation suggests that HSPA8 may act as a membrane chaperone.

Indexed as

CardiolipinsCell MembraneHeat-Shock ProteinsHeat-Shock ResponseHSC70 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansLiposomesMolecular ChaperonesPhospholipidsCardiolipinsHeat-Shock ProteinsHSC70 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHSPA8 protein, humanLiposomesMolecular ChaperonesPhospholipidsChaperonesHsp70HSP90AA1HSPA1AHSPA8LiposomesMembranesPhospholipids

Identifiers

PMID34003451
PMCPMC8129608
OpenAlexW3160873027

What OpenQuestion holds

Textmetadata
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 OpenQuestion graph.