Evidence map›Paper›PMID 17030621›Full record

ArticleMolecular and cellular biology2007

Loss of Hsp90 association up-regulates Src-dependent ErbB2 activity.

Wanping Xu, Xitong Yuan, Kristin Beebe, Zhexin Xiang, Len Neckers

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

37 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches.Trends in biochemical sciences · 2017
    Review
  9. Article
  10. Article
  11. Role of Erbin in ErbB2-dependent breast tumor growth.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  12. Review
  13. Article
  14. HSP90: chaperone-me-not.Pathology oncology research : POR · 2013
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  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

5 authors at 2 institutions in 2 countries.

Wanping XuUrologic Oncology Branch, Center for Cancer Research, National Cancer Institute, 9000 Rockville Pike, Bethesda, MD 20892-1107, USA.
Xitong Yuan
Kristin Beebe
Zhexin Xiang
Len Neckers
Cancer Institute (WIA) · INNational Institutes of Health · US

Funding

Role of HSP90 Family Chaperone Proteins in Cellular Signal TransductionZIASC010074 · NCI · DIVISION OF CLINICAL SCIENCES - NCI · PI NECKERS, LEONARD · 2009 to 2025
$13.3M
Simulating Protein Structures, Complexes, And DynamicsZIACT000265 · CIT · CENTER FOR INFORMATION TECHNOLOGY · PI STEINBACH, PETER J · 2009 to 2020
$8.2M
ROLE OF HSP90/GFP94 CHAPERONE PROTEINS IN CELLULAR SIGNAL TRANSDUCTIONZ01SC010074 · SC · DIVISION OF CLINICAL SCIENCES - NCI · PI NECKERS, LEONARD · 1996 to 2008
$3.7M
SIMULATING PROTEIN STRUCTURES, COMPLEXES, AND DYNAMICSZ01CT000265 · CIT · COMPUTER RESEARCH AND TECHNOLOGY · PI STEINBACH, PETER J · 1997 to 2008
$1.3M
6 · The paper itself

Abstract

The receptor tyrosine kinase ErbB2 plays a crucial role in tumorigenesis. We showed previously that the molecular chaperone Hsp90 protects ErbB2 from proteasome-mediated degradation by binding to a short loop structure in the N-lobe of the kinase domain. Here we show that loss of Hsp90 binding correlates with enhanced ErbB2 kinase activity and its transactivating potential, concomitant with constitutively increased phosphorylation of Tyr877, located in the activation loop of the kinase domain. We show further that Tyr877 phosphorylation is mediated by Src and that it is necessary for the enhanced kinase activity of ErbB2. Finally, computer modeling of the kinase domain suggests a phosphorylation-dependent reorientation of the activation loop, denoting the importance of Tyr877 phosphorylation for ErbB2 activity. These findings suggest that Hsp90 binding to ErbB2 participates in regulation of kinase activity as well as kinase stability.

Indexed as

Gene Expression Regulation, EnzymologicUp-Regulation3T3 CellsAmino Acid SequenceAnimalsChlorocebus aethiopsCOS CellsErb-b2 Receptor Tyrosine KinasesHSP90 Heat-Shock ProteinsHumansMiceMolecular Sequence DataProteasome Endopeptidase ComplexProtein Bindingsrc-Family KinasesTyrosineErb-b2 Receptor Tyrosine KinasesHSP90 Heat-Shock ProteinsProteasome Endopeptidase Complexsrc-Family KinasesTyrosine

Identifiers

PMID17030621
PMCPMC1800645
OpenAlexW2133519534

What OpenQuestion holds

Textmetadata
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.