Evidence map›Paper›PMID 28447215›Full record

ArticleCell stress & chaperones2017

Interplay between recombinant Hsp70 and proteasomes: proteasome activity modulation and ubiquitin-independent cleavage of Hsp70.

Alexey V Morozov, Tatiana M Astakhova, David G Garbuz, George S Krasnov, Natalia V Bobkova, Olga G Zatsepina, Vadim L Karpov, Michail B Evgen'ev

Open access · bronzeAbstract read
In one paragraph

Article in Cell stress & chaperones, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 39 citations in OpenAlex.

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  11. Immunoproteasome Inhibitor ONX-0914 Affects Long-Term Potentiation in Murine Hippocampus.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2021
    Article
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  13. Review
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  15. Article
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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

8 authors at 3 institutions in 1 country.

Alexey V MorozovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow, 119991, Russia. Runkel@inbox.ru.ORCID http://orcid.org/0000-0003-4310-8073
Tatiana M AstakhovaKoltzov Institute of Developmental Biology, Russian Academy of Sciences, Vavilov str. 26, Moscow, 124319, Russia.
David G GarbuzEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow, 119991, Russia.
George S KrasnovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow, 119991, Russia.
Natalia V BobkovaInstitute of Cell Biophysics, Russian Academy of Sciences, Pushchino, Institutskaya st. 3, Pushchino, Moscow Region, 142290, Russia.
Olga G ZatsepinaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow, 119991, Russia.
Vadim L KarpovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow, 119991, Russia.
Michail B Evgen'evEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow, 119991, Russia.
Engelhardt Institute of Molecular Biology · RUInstitute of Cell Biophysics · RUKoltzov Institute of Developmental Biology · RU

Funding

Ministry of Education and Science of the Russian Federation 14.Z50.31.0014Russian President foundation grant МК-3613.2017.4Russian Science Foundation (RU) 14-50-00060
6 · The paper itself

Abstract

The heat shock protein 70 (Hsp70, human HSPA1A) plays indispensable roles in cellular stress responses and protein quality control (PQC). In the framework of PQC, it cooperates with the ubiquitin-proteasome system (UPS) to clear damaged and dysfunctional proteins in the cell. Moreover, Hsp70 itself is rapidly degraded following the recovery from stress. It was demonstrated that its fast turnover is mediated via ubiquitination and subsequent degradation by the 26S proteasome. At the same time, the effect of Hsp70 on the functional state of proteasomes has been insufficiently investigated. Here, we characterized the direct effect of recombinant Hsp70 on the activity of 20S and 26S proteasomes and studied Hsp70 degradation by the 20S proteasome in vitro. We have shown that the activity of purified 20S proteasomes is decreased following incubation with recombinant human Hsp70. On the other hand, high concentrations of Hsp70 activated 26S proteasomes. Finally, we obtained evidence that in addition to previously reported ubiquitin-dependent degradation, Hsp70 could be cleaved independent of ubiquitination by the 20S proteasome. The results obtained reveal novel aspects of the interplay between Hsp70 and proteasomes.

Indexed as

Cell LineElectrophoresis, Polyacrylamide GelHSP70 Heat-Shock ProteinsHumansProteasome Endopeptidase ComplexRecombinant ProteinsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationUbiquitinATP dependent 26S proteaseHSP70 Heat-Shock ProteinsProteasome Endopeptidase ComplexRecombinant ProteinsUbiquitinHeat shock proteinsHsp70ProteasomeProteasome regulatorsUbiquitin-independent degradation

Identifiers

PMID28447215
PMCPMC5573687
OpenAlexW2609595109

What OpenQuestion holds

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Registered trials

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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.