Evidence map›Paper›PMID 24608665›Full record

ArticlePloS one2014

Hsp90-dependent assembly of the DBC2/RhoBTB2-Cullin3 E3-ligase complex.

Jacob R Manjarrez, Liang Sun, Thomas Prince, Robert L Matts

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

16 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Genotype-phenotype correlations in RHOBTB2-associated neurodevelopmental disorders.Genetics in medicine : official journal of the American College of Medical Genetics · 2023
    Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. PPARγ and RhoBTB1 in hypertension.Current opinion in nephrology and hypertension · 2020
    Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Review
  16. 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

4 authors at 1 institution in 1 country.

Jacob R ManjarrezDepartment of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, Oklahoma, United States of America.
Liang SunDepartment of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, Oklahoma, United States of America.
Thomas PrinceDepartment of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, Oklahoma, United States of America.
Robert L MattsDepartment of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, Oklahoma, United States of America.
Oklahoma State University · US

Funding

Identification of Natural Product Inhibitors of Hsp90 as Chemotherapeutic AgentsR01CA125392 · NCI · OKLAHOMA STATE UNIVERSITY STILLWATER · PI MATTS, ROBERT L. · 2007 to 2010
$994k
NCI NIH HHS 3R01CA125392-03S109NCI NIH HHS R01 CA125392
6 · The paper itself

Abstract

The expression of the wild-type tumor-suppressor gene DBC2 (Deleted-in-Breast Cancer 2, a.k.a RhoBTB2) is suppressed in many cancers, in addition to breast cancer. In a screen for Cdc37-associated proteins, DBC2 was identified to be a potential client protein of the 90 kDa heat shock protein (Hsp90) chaperone machine. Pull down assays of ectopically expressed DBC2 confirmed that DBC2 associated with Hsp90 and its co-chaperone components in reticulocyte lysate and MCF7 cells. Similar to other atypical Rho GTPases, DBC2 was found to have retained the capacity to bind GTP. The ability of DBC2 to bind GTP was modulated by the Hsp90 ATPase cycle, as demonstrated through the use of the Hsp90 chemical inhibitors, geldanamycin and molybdate. The binding of full length DBC2 to GTP was suppressed in the presence of geldanamycin, while it was enhanced in the presence of molybdate. Furthermore, assembly of DBC2-Cullin3-COP9 E3 ligase complexes was Hsp90-dependent. The data suggest a new paradigm for Hsp90-modulated assembly of a Cul3/DBC2 E3 ubiquitin ligase complex that may extend to other E3 ligase complexes.

Indexed as

Cell LineCullin ProteinsGTP-Binding ProteinsHSP90 Heat-Shock ProteinsHumansImmunoprecipitationMass SpectrometryProtein BindingTumor Suppressor ProteinsUbiquitin-Protein LigasesCUL3 protein, humanCullin ProteinsGTP-Binding ProteinsHSP90 Heat-Shock ProteinsRHOBTB2 protein, humanTumor Suppressor ProteinsUbiquitin-Protein Ligases

Identifiers

PMID24608665
PMCPMC3946479
OpenAlexW2072982665

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.