Evidence map›Paper›PMID 25504578›Full record

ArticleEMBO reports2015

Hop/Sti1 phosphorylation inhibits its co-chaperone function.

Alina Röhl, Franziska Tippel, Evelyn Bender, Andreas B Schmid, Klaus Richter, Tobias Madl, Johannes Buchner

Open access · hybridAbstract read
In one paragraph

Article in EMBO reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

19 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Fine Tuning: Effects of Post-Translational Modification on Hsp70 Chaperones.International journal of molecular sciences · 2019
    Review
  14. Article
  15. Article
  16. The HSP90 chaperone machinery.Nature reviews. Molecular cell biology · 2017
    Review
  17. Review
  18. Article
  19. 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

7 authors at 3 institutions in 2 countries.

Alina RöhlCenter for Integrated Protein Science (CIPSM) at the Department Chemie, Technische Universität München, Garching, Germany.
Franziska TippelCenter for Integrated Protein Science (CIPSM) at the Department Chemie, Technische Universität München, Garching, Germany.
Evelyn BenderCenter for Integrated Protein Science (CIPSM) at the Department Chemie, Technische Universität München, Garching, Germany.
Andreas B SchmidCenter for Integrated Protein Science (CIPSM) at the Department Chemie, Technische Universität München, Garching, Germany.
Klaus RichterCenter for Integrated Protein Science (CIPSM) at the Department Chemie, Technische Universität München, Garching, Germany.
Tobias MadlCenter for Integrated Protein Science (CIPSM) at the Department Chemie, Technische Universität München, Garching, Germany Institute of Structural Biology Helmholtz Zentrum München, Neuherberg, Germany Institute of Molecular Biology & Biochemistry, Center of Molecular Medicine, Medical University of Graz, Graz, Austria.
Johannes BuchnerCenter for Integrated Protein Science (CIPSM) at the Department Chemie, Technische Universität München, Garching, Germany johannes.buchner@tum.de.
Center for Integrated Protein Science Munich · DETechnical University of Munich · DEHelmholtz Zentrum München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotes, the molecular chaperones Hsp90 and Hsp70 are connected via the co-chaperone Sti1/Hop, which allows transfer of clients. Here, we show that the basic functions of yeast Sti1 and human Hop are conserved. These include the simultaneous binding of Hsp90 and Hsp70, the inhibition of the ATPase activity of Hsp90, and the ability to support client activation in vivo. Importantly, we reveal that both Hop and Sti1 are subject to inhibitory phosphorylation, although the sites modified and the influence of regulatory phosphorylation is species specific. Phospho-mimetic variants have a reduced ability to activate clients in vivo and different affinity for Hsp70. Hop is more tightly regulated, as phosphorylation affects also the interaction with Hsp90 and induces structural rearrangements in the core part of the protein.

Indexed as

Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansMolecular ChaperonesPhosphorylationProtein BindingHeat-Shock ProteinsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMolecular Chaperonesco‐chaperonephosphorylationregulationSAXSSti1/Hop

Identifiers

PMID25504578
PMCPMC4328751
OpenAlexW2113170630

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.