Evidence map›Paper›PMID 17194752›Full record

ArticleMolecular and cellular biology2007

Phosphorylation of MNAR promotes estrogen activation of phosphatidylinositol 3-kinase.

James G Greger, Natalie Fursov, Neil Cooch, Sean McLarney, Leonard P Freedman, Dean P Edwards, Boris J Cheskis

RetractedOpen access · greenAbstract readRetracted Publication
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. It has been retracted, and should not be counted. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

20 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Cytoplasmic estrogen receptor in breast cancer.Clinical cancer research : an official journal of the American Association for Cancer Research · 2012
    Article
  5. Acetylation and nuclear receptor action.The Journal of steroid biochemistry and molecular biology · 2011
    Review
  6. Article
  7. Review
  8. Regulation of aromatase induction by nuclear receptor coregulator PELP1.The Journal of steroid biochemistry and molecular biology · 2010
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. PELP1--a novel estrogen receptor-interacting protein.Molecular and cellular endocrinology · 2008
    Review
  16. Article
  17. Cracking the coregulator codes.Current opinion in cell biology · 2008
    Review
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

James G GregerWomen's Health and Musculoskeletal Biology, Wyeth Research, Nuclear Receptors, 500 Arcola Road, Collegeville, PA 19426, USA.
Natalie Fursov
Neil Cooch
Sean McLarney
Leonard P Freedman
Dean P Edwards
Boris J Cheskis
Baylor College of Medicine · USWomen's Health Research Institute · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Estrogen actions are mediated by a complex interface of direct control of gene expression (the so-called "genomic action") and by regulation of cell signaling/phosphorylation cascades, referred to as the "nongenomic," or extranuclear, action. We have previously described the identification of MNAR (modulator of nongenomic action of estrogen receptor) as a novel scaffold protein that regulates estrogen receptor alpha (ERalpha) activation of cSrc. In this study, we have investigated the role of MNAR in 17beta-estradiol (E2)-induced activation of the phosphatidylinositol 3-kinase (PI3K)/Akt pathway. Consistent with our previous results, a direct correlation was established between MNAR expression levels and E2-induced activation of PI3 and Akt kinases. Endogenous MNAR, ERalpha, cSrc, and p85, the regulatory subunit of PI3 kinase, interacted in MCF7 cells treated with E2. The interaction between p85 and MNAR required activation of cSrc and MNAR phosphorylation on Tyr 920. Consequently, the mutation of this tyrosine to alanine (Y920A) abrogated the interaction between MNAR and p85 and the E2-induced activation of the PI3K/Akt pathway, which was required for the E2-induced protection of MCF7 cells from apoptosis. Nonetheless, the Y920A mutant potentiated the E2-induced activation of the Src/MAPK pathway and MCF7 cell proliferation, as observed with the wild-type MNAR. These results provide new and important insights into the molecular mechanisms of E2-induced regulation of cell proliferation and apoptosis.

Indexed as

AlanineAmino Acid SubstitutionAnimalsApoptosisBreast NeoplasmsCell Line, TumorChlorocebus aethiopsCOS CellsEnzyme ActivationEstradiolEstrogen Receptor alphaEstrogensFemaleGreen Fluorescent ProteinsHumansImmunoprecipitationAlanineEstradiolEstrogen Receptor alphaEstrogensGreen Fluorescent ProteinsPhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktReceptors, EstrogenRNA, Small Interferingsrc-Family KinasesTyrosine

Identifiers

PMID17194752
PMCPMC1820473
OpenAlexW2120351762

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.