Evidence map›Paper›PMID 26693507›Full record

ArticleData in brief2015

The dynamic interactome of human Aha1 upon Y223 phosphorylation.

Donald Wolfgeher, Diana M Dunn, Mark R Woodford, Dimitra Bourboulia, Gennady Bratslavsky, Mehdi Mollapour, Stephen J Kron, Andrew W Truman

Open access · goldAbstract read
In one paragraph

Article in Data in brief, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact, top 93% 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

10 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. The role of Aha1 in cancer and neurodegeneration.Frontiers in molecular neuroscience · 2024
    Review
  3. Review
  4. Sel1-like proteins and peptides are the majorAmerican journal of physiology. Cell physiology · 2023
    Article
  5. Biomarkers of Pediatric Cataracts: A Proteomics Analysis of Aqueous Fluid.International journal of molecular sciences · 2023
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. 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

8 authors at 4 institutions in 1 country.

Donald WolfgeherDepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, IL 60637, USA.
Diana M DunnDepartment of Urology, SUNY Upstate Medical University, Syracuse, NY 13210, USA ; Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, NY 13210, USA ; Cancer Research Institute, SUNY Upstate Medical University, Syracuse, NY 13210, USA.
Mark R WoodfordDepartment of Urology, SUNY Upstate Medical University, Syracuse, NY 13210, USA ; Cancer Research Institute, SUNY Upstate Medical University, Syracuse, NY 13210, USA.
Dimitra BourbouliaDepartment of Urology, SUNY Upstate Medical University, Syracuse, NY 13210, USA ; Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, NY 13210, USA ; Cancer Research Institute, SUNY Upstate Medical University, Syracuse, NY 13210, USA.
Gennady BratslavskyDepartment of Urology, SUNY Upstate Medical University, Syracuse, NY 13210, USA ; Cancer Research Institute, SUNY Upstate Medical University, Syracuse, NY 13210, USA.
Mehdi MollapourDepartment of Urology, SUNY Upstate Medical University, Syracuse, NY 13210, USA ; Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, NY 13210, USA ; Cancer Research Institute, SUNY Upstate Medical University, Syracuse, NY 13210, USA.
Stephen J KronDepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, IL 60637, USA.
Andrew W TrumanDepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, IL 60637, USA ; Department of Biological Sciences, University of North Carolina at Charlotte, Charlotte, NC 28223, USA.
SUNY Upstate Medical University · USCancer Research Institute · USUniversity of Chicago · USUniversity of North Carolina at Charlotte · US

Funding

Radiation response within the tumor microenvironmentR01CA164492 · NCI · UNIVERSITY OF CHICAGO · PI KRON, STEPHEN J. · 2011 to 2015
$4.8M
NCI NIH HHS R01 CA164492
6 · The paper itself

Abstract

Heat Shock Protein 90 (Hsp90) is an essential chaperone that supports the function of a wide range of signaling molecules. Hsp90 binds to a suite of co-chaperone proteins that regulate Hsp90 function through alteration of intrinsic ATPase activity. Several studies have determined Aha1 to be an important co-chaperone whose binding to Hsp90 is modulated by phosphorylation, acetylation and SUMOylation of Hsp90 [1], [2]. In this study, we applied quantitative affinity-purification mass spectrometry (AP-MS) proteomics to understand how phosphorylation of hAha1 at Y223 altered global client/co-chaperone interaction [3]. Specifically, we characterized and compared the interactomes of Aha1-Y223F (phospho-mutant form) and Aha1-Y223E (phospho-mimic form). We identified 99 statistically significant interactors of hAha1, a high proportion of which (84%) demonstrated preferential binding to the phospho-mimic form of hAha1. The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository [4] with the dataset identifier PXD001737.

Indexed as

Aha1CancerChaperonesCo-chaperonesHsp90InteractomePhosphorylationProteomics

Identifiers

PMID26693507
PMCPMC4659802
OpenAlexW2192321209

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.