Evidence map›Paper›PMID 29343704›Full record

ArticleNature communications2018

Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation.

Ashleigh B Bachman, Dimitra Keramisanou, Wanping Xu, Kristin Beebe, Michael A Moses, M V Vasantha Kumar, Geoffrey Gray, Radwan Ebna Noor, Arjan van der Vaart, Len Neckers and 1 more

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

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

28 citing papers in PubMed, 52 citations in OpenAlex.

  1. Cysteine thiol-to-sulfonate oxidation induces unfolding for the functional switching of the extracellular HMGB1 protein.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  12. Article
  13. Thermal Proteome Profiling Reveals the O-GlcNAc-Dependent Meltome.Journal of the American Chemical Society · 2022
    Article
  14. Review
  15. General Structural and Functional Features of Molecular Chaperones.Advances in experimental medicine and biology · 2021
    Article
  16. Article
  17. Review
  18. A Chemical Biology Approach to the Chaperome in Cancer-HSP90 and Beyond.Cold Spring Harbor perspectives in biology · 2020
    Review
  19. Review
  20. 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

11 authors at 2 institutions in 1 country.

Ashleigh B BachmanDepartment of Chemistry, University of South Florida, Tampa, FL, 33620, USA.
Dimitra KeramisanouDepartment of Chemistry, University of South Florida, Tampa, FL, 33620, USA.
Wanping XuUrologic Oncology Branch, National Cancer Institute, Bethesda, MD, 20892, USA.
Kristin BeebeUrologic Oncology Branch, National Cancer Institute, Bethesda, MD, 20892, USA.
Michael A MosesUrologic Oncology Branch, National Cancer Institute, Bethesda, MD, 20892, USA.
M V Vasantha KumarDepartment of Chemistry, University of South Florida, Tampa, FL, 33620, USA.
Geoffrey GrayDepartment of Chemistry, University of South Florida, Tampa, FL, 33620, USA.
Radwan Ebna NoorDepartment of Chemistry, University of South Florida, Tampa, FL, 33620, USA.
Arjan van der VaartDepartment of Chemistry, University of South Florida, Tampa, FL, 33620, USA.
Len NeckersUrologic Oncology Branch, National Cancer Institute, Bethesda, MD, 20892, USA.
Ioannis GelisDepartment of Chemistry, University of South Florida, Tampa, FL, 33620, USA. igelis@usf.edu.
University of South Florida · USNational Cancer Institute · US

Funding

Post-translational modifications of Hsp90 that impact drug efficacyZIABC011032 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NECKERS, LEONARD · 2009 to 2025
$11.5M
ROLE OF HSP90/GFP94 CHAPERONE PROTEINS IN CELLULAR SIGNAL TRANSDUCTIONZ01SC010074 · SC · DIVISION OF CLINICAL SCIENCES - NCI · PI NECKERS, LEONARD · 1996 to 2008
$3.7M
Assembly mechanism of cochaperone-kinase complexesR01GM115854 · NIGMS · UNIVERSITY OF SOUTH FLORIDA · PI GELIS, IOANNIS · 2015 to 2019
$1.6M
Intramural NIH HHS Z01 SC010074NIGMS NIH HHS R01 GM115854
6 · The paper itself

Abstract

During the Hsp90-mediated chaperoning of protein kinases, the core components of the machinery, Hsp90 and the cochaperone Cdc37, recycle between different phosphorylation states that regulate progression of the chaperone cycle. We show that Cdc37 phosphorylation at Y298 results in partial unfolding of the C-terminal domain and the population of folding intermediates. Unfolding facilitates Hsp90 phosphorylation at Y197 by unmasking a phosphopeptide sequence, which serves as a docking site to recruit non-receptor tyrosine kinases to the chaperone complex via their SH2 domains. In turn, Hsp90 phosphorylation at Y197 specifically regulates its interaction with Cdc37 and thus affects the chaperoning of only protein kinase clients. In summary, we find that by providing client class specificity, Hsp90 cochaperones such as Cdc37 do not merely assist in client recruitment but also shape the post-translational modification landscape of Hsp90 in a client class-specific manner.

Indexed as

Cell Cycle ProteinsChaperoninsHSP90 Heat-Shock ProteinsHumansPhosphorylationProtein FoldingProtein-Tyrosine Kinasessrc Homology DomainsCDC37 protein, humanCell Cycle ProteinsChaperoninsHSP90 Heat-Shock ProteinsProtein-Tyrosine Kinases

Identifiers

PMID29343704
PMCPMC5772613
OpenAlexW2783162131

What OpenQuestion 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 OpenQuestion graph.