Evidence map›Paper›PMID 26392412›Full record

ArticleG3 (Bethesda, Md.)2015

Proteomic Analysis of Dhh1 Complexes Reveals a Role for Hsp40 Chaperone Ydj1 in Yeast P-Body Assembly.

Gregory A Cary, Dani B N Vinh, Patrick May, Rolf Kuestner, Aimée M Dudley

Open access · goldAbstract read
In one paragraph

Article in G3 (Bethesda, Md.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

12 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Composition-based prediction and rational manipulation of prion-like domain recruitment to stress granules.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. The sole LSm complex inRNA (New York, N.Y.) · 2017
    Article
  11. Article
  12. 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

5 authors at 2 institutions in 2 countries.

Gregory A CaryInstitute for Systems Biology, Seattle, Washington 98109 Molecular and Cellular Biology Program, University of Washington, Seattle, Washington 98195.ORCID http://orcid.org/0000-0003-3573-5229
Dani B N VinhInstitute for Systems Biology, Seattle, Washington 98109.ORCID http://orcid.org/0000-0002-4139-6860
Patrick MayInstitute for Systems Biology, Seattle, Washington 98109 Luxembourg Centre for Systems Biomedicine, Université du Luxembourg, Esch-sur-Alzette, Luxembourg L-4362.
Rolf KuestnerInstitute for Systems Biology, Seattle, Washington 98109.
Aimée M DudleyMolecular and Cellular Biology Program, University of Washington, Seattle, Washington 98195 Pacific Northwest Diabetes Research Institute, Seattle, Washington 98122 aimee.dudley@gmail.com.ORCID http://orcid.org/0000-0003-3644-0625
Institute for Systems Biology · USUniversity of Washington · US

Funding

Quantitative Systems BiologyP50GM076547 · NIGMS · INSTITUTE FOR SYSTEMS BIOLOGY · PI OZINSKY, ADRIAN · 2006 to 2016
$30.6M
Temporal and spatial effects on expression and functionK22HG002908 · NHGRI · INSTITUTE FOR SYSTEMS BIOLOGY · PI DUDLEY, AIMEE M · 2003 to 2009
$1.1M
NHLBI PROTEOMICS INITIATIVE-268028179N01HV028179 · HV · INSTITUTE FOR SYSTEMS BIOLOGY · 2002 to 2002
–
NHGRI NIH HHS K22 HG002908NHLBI NIH HHS N01 HV028179NHLBI NIH HHS N01-HV-28179NIGMS NIH HHS P50 GM076547
6 · The paper itself

Abstract

P-bodies (PB) are ribonucleoprotein (RNP) complexes that aggregate into cytoplasmic foci when cells are exposed to stress. Although the conserved mRNA decay and translational repression machineries are known components of PB, how and why cells assemble RNP complexes into large foci remain unclear. Using mass spectrometry to analyze proteins immunoisolated with the core PB protein Dhh1, we show that a considerable number of proteins contain low-complexity sequences, similar to proteins highly represented in mammalian RNP granules. We also show that the Hsp40 chaperone Ydj1, which contains an low-complexity domain and controls prion protein aggregation, is required for the formation of Dhh1-GFP foci on glucose depletion. New classes of proteins that reproducibly coenrich with Dhh1-GFP during PB induction include proteins involved in nucleotide or amino acid metabolism, glycolysis, transfer RNA aminoacylation, and protein folding. Many of these proteins have been shown to form foci in response to other stresses. Finally, analysis of RNA associated with Dhh1-GFP shows enrichment of mRNA encoding the PB protein Pat1 and catalytic RNAs along with their associated mitochondrial RNA-binding proteins. Thus, global characterization of PB composition has uncovered proteins important for PB assembly and evidence suggesting an active role for RNA in PB function.

Indexed as

DEAD-box RNA HelicasesHSP40 Heat-Shock ProteinsProtein BindingProteomeRibonucleoproteinsRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDEAD-box RNA HelicasesDHH1 protein, S cerevisiaeHSP40 Heat-Shock ProteinsPAT1 protein, S cerevisiaeProteomeRibonucleoproteinsRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsYDJ1 protein, S cerevisiaechaperonesmicroarraysP-bodiesproteomics

Identifiers

PMID26392412
PMCPMC4632068
OpenAlexW2180829375

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.