Evidence map›Paper›PMID 19635806›Full record

ArticleMolecular and cellular biology2009

p85 Associates with unphosphorylated PTEN and the PTEN-associated complex.

Rosalia Rabinovsky, Panisa Pochanard, Chontelle McNear, Saskia M Brachmann, Jonathan S Duke-Cohan, Levi A Garraway, William R Sellers

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
3.6field-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

56 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Article
  3. The orchestrated signaling by PI3Kα and PTEN at the membrane interface.Computational and structural biotechnology journal · 2022
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Emerging Roles of BRD7 in Pathophysiology.International journal of molecular sciences · 2020
    Review
  9. Review
  10. Review
  11. mNature metabolism · 2019
    Article
  12. PIP4K2A as a negative regulator of PI3K in PTENThe Journal of experimental medicine · 2019
    Article
  13. Review
  14. Review
  15. Regulation and modulation of PTEN activity.Molecular biology reports · 2018
    Review
  16. Review
  17. Article
  18. Article
  19. PI3K-p110α mediates the oncogenic activity induced by loss of the novel tumor suppressor PI3K-p85α.Proceedings of the National Academy of Sciences of the United States of America · 2017
    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

7 authors at 4 institutions in 1 country.

Rosalia RabinovskyDepartment of Medical Oncology, Dana-Farber Cancer Institute, 44 Binney St., Boston, MA 02115, USA.
Panisa Pochanard
Chontelle McNear
Saskia M Brachmann
Jonathan S Duke-Cohan
Levi A Garraway
William R Sellers
Dana-Farber Cancer Institute · USHarvard University · USBroad Institute · USDana-Farber Brigham Cancer Center · US

Funding

FUNCTIONAL ANALYSIS OF THE PTEN TUMOR SUPPRESSOR PROTEINR01CA085912 · NCI · DANA-FARBER CANCER INSTITUTE · PI GARRAWAY, LEVI A. · 2000 to 2009
$2.7M
NCI NIH HHS R01 CA085912
6 · The paper itself

Abstract

The lipid phosphatase PTEN functions as a tumor suppressor by dephosphorylating the D3 position of phosphoinositide-3,4,5-trisphosphate, thereby negatively regulating the phosphoinositide 3-kinase (PI3K)/AKT signaling pathway. In mammalian cells, PTEN exists either as a monomer or as a part of a >600-kDa complex (the PTEN-associated complex [PAC]). Previous studies suggest that the antagonism of PI3K/AKT signaling by PTEN may be mediated by a nonphosphorylated form of the protein resident within the multiprotein complex. Here we show that PTEN associates with p85, the regulatory subunit of PI3K. Using newly generated antibodies, we demonstrate that this PTEN-p85 association involves the unphosphorylated form of PTEN engaged within the PAC and also includes the p110beta isoform of PI3K. The PTEN-p85 association is enhanced by trastuzumab treatment and linked to a decline in AKT phosphorylation in some ERBB2-amplified breast cancer cell lines. Together, these results suggest that integration of p85 into the PAC may provide a novel means of downregulating the PI3K/AKT pathway.

Indexed as

Amino Acid SequenceAntibodiesCell LineErb-b2 Receptor Tyrosine KinasesHumansMolecular Sequence DataMolecular WeightPhosphatidylinositol 3-KinasesPhosphorylationProtein BindingProtein SubunitsPTEN PhosphohydrolaseAntibodiesErb-b2 Receptor Tyrosine KinasesPhosphatidylinositol 3-KinasesProtein SubunitsPTEN PhosphohydrolasePTEN protein, human

Identifiers

PMID19635806
PMCPMC2747981
OpenAlexW2168286074

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.