Evidence map›Paper›PMID 25316598›Full record

ArticleGenome biology and evolution2014

The Hsp90-dependent proteome is conserved and enriched for hub proteins with high levels of protein-protein connectivity.

Rajaneesh Karimpurath Gopinath, Shu-Ting You, Kun-Yi Chien, Krishna B S Swamy, Jau-Song Yu, Scott C Schuyler, Jun-Yi Leu

Open access · goldAbstract read
In one paragraph

Article in Genome biology and evolution, 2014. 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
1.4field-weighted citation impact, top 18% 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, 31 citations in OpenAlex.

  1. Tick-Tock: Cancer Cell Division Cycle Clocks Strike Midnight.International journal of molecular sciences · 2025
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  4. Insights into Hsp90 mechanism andFrontiers in molecular biosciences · 2024
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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

7 authors at 4 institutions in 1 country.

Rajaneesh Karimpurath GopinathMolecular and Cell Biology, Taiwan International Graduate Program, Graduate Institute of Life Sciences, National Defense Medical Center and Academia Sinica Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan schuyler@mail.cgu.edu.tw jleu@imb.sinica.edu.tw.
Shu-Ting YouMolecular and Cell Biology, Taiwan International Graduate Program, Graduate Institute of Life Sciences, National Defense Medical Center and Academia Sinica Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan schuyler@mail.cgu.edu.tw jleu@imb.sinica.edu.tw.
Kun-Yi ChienMolecular Medicine Research Center, Department of Biochemistry and Molecular Biology, College of Medicine, Chang Gung University, Tao-Yuan, Taiwan schuyler@mail.cgu.edu.tw jleu@imb.sinica.edu.tw.
Krishna B S SwamyInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan.
Jau-Song YuDepartment of Cell and Molecular Biology, College of Medicine, Chang Gung University, Tao-Yuan, Taiwan.
Scott C SchuylerDepartment of Biomedical Sciences, College of Medicine, Chang Gung University, Tao-Yuan, Taiwan schuyler@mail.cgu.edu.tw jleu@imb.sinica.edu.tw.
Jun-Yi LeuInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan schuyler@mail.cgu.edu.tw jleu@imb.sinica.edu.tw.
Chang Gung University · TWInstitute of Molecular Biology, Academia Sinica · TWAcademia Sinica · TWNational Defense Medical Center · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hsp90 is one of the most abundant and conserved proteins in the cell. Reduced levels or activity of Hsp90 causes defects in many cellular processes and also reveals genetic and nongenetic variation within a population. Despite information about Hsp90 protein-protein interactions, a global view of the Hsp90-regulated proteome in yeast is unavailable. To investigate the degree of dependency of individual yeast proteins on Hsp90, we used the "stable isotope labeling by amino acids in cell culture" method coupled with mass spectrometry to quantify around 4,000 proteins in low-Hsp90 cells. We observed that 904 proteins changed in their abundance by more than 1.5-fold. When compared with the transcriptome of the same population of cells, two-thirds of the misregulated proteins were observed to be affected posttranscriptionally, of which the majority were downregulated. Further analyses indicated that the downregulated proteins are highly conserved and assume central roles in cellular networks with a high number of protein interacting partners, suggesting that Hsp90 buffers genetic and nongenetic variation through regulating protein network hubs. The downregulated proteins were enriched for essential proteins previously not known to be Hsp90-dependent. Finally, we observed that downregulation of transcription factors and mating pathway components by attenuating Hsp90 function led to decreased target gene expression and pheromone response, respectively, providing a direct link between observed proteome regulation and cellular phenotypes.

Indexed as

AnimalsGenomicsHSP90 Heat-Shock ProteinsHumansProtein BindingProteomicsSaccharomyces cerevisiaeHSP90 Heat-Shock Proteinsgenetic bufferingmolecular chaperoneprotein networkyeast genomicsyeast proteomics

Identifiers

PMID25316598
PMCPMC4224352
OpenAlexW2144310643

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.