Evidence map›Paper›PMID 10958682›Full record

ArticleMolecular and cellular biology2000

5' phospholipid phosphatase SHIP-2 causes protein kinase B inactivation and cell cycle arrest in glioblastoma cells.

V Taylor, M Wong, C Brandts, L Reilly, N M Dean, L M Cowsert, S Moodie, D Stokoe

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

51 citing papers in PubMed, 185 citations in OpenAlex.

  1. Article
  2. Article
  3. A spatially organizedScience advances · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. When PIPFrontiers in cell and developmental biology · 2022
    Review
  8. PTEN and Other PtdIns(3,4,5)PInternational journal of molecular sciences · 2020
    Review
  9. Article
  10. Endothelial dysfunction due to selective insulin resistance in vascular endothelium: insights from mechanistic modeling.American journal of physiology. Endocrinology and metabolism · 2020 · on this map
    Article
  11. Article
  12. Article
  13. Article
  14. PI(3,4)PCancer science · 2017
    Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. 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 3 institutions in 1 country.

V TaylorCancer Research Institute, University of California, San Francisco 94115, USA.
M Wong
C Brandts
L Reilly
N M Dean
L M Cowsert
S Moodie
D Stokoe
University of California, San Francisco · USIonis Pharmaceuticals (United States) · USCancer Research Institute · US

Funding

PROTEIN KINASE B PATHWAY IN CELL TRANSFORMATIONR01CA079548 · NCI · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI STOKOE, DAVID H · 1999 to 2002
$651k
NCI NIH HHS R01CA79548
6 · The paper itself

Abstract

The tumor suppressor protein PTEN is mutated in glioblastoma multiform brain tumors, resulting in deregulated signaling through the phosphoinositide 3-kinase (PI3K)-protein kinase B (PKB) pathway, which is critical for maintaining proliferation and survival. We have examined the relative roles of the two major phospholipid products of PI3K activity, phosphatidylinositol 3,4-biphosphate [PtdIns(3,4)P2] and phosphatidylinositol 3,4,5-triphosphate [PtdIns(3,4,5)P3], in the regulation of PKB activity in glioblastoma cells containing high levels of both of these lipids due to defective PTEN expression. Reexpression of PTEN or treatment with the PI3K inhibitor LY294002 abolished the levels of both PtdIns(3, 4)P2 and PtdIns(3,4,5)P3, reduced phosphorylation of PKB on Thr308 and Ser473, and inhibited PKB activity. Overexpression of SHIP-2 abolished the levels of PtdIns(3,4,5)P3, whereas PtdIns(3,4)P2 levels remained high. However, PKB phosphorylation and activity were reduced to the same extent as they were with PTEN expression. PTEN and SHIP-2 also significantly decreased the amount of PKB associated with cell membranes. Reduction of SHIP-2 levels using antisense oligonucleotides increased PKB activity. SHIP-2 became tyrosine phosphorylated following stimulation by growth factors, but this did not significantly alter its phosphatase activity or ability to antagonize PKB activation. Finally we found that SHIP-2, like PTEN, caused a potent cell cycle arrest in G(1) in glioblastoma cells, which is associated with an increase in the stability of expression of the cell cycle inhibitor p27(KIP1). Our results suggest that SHIP-2 plays a negative role in regulating the PI3K-PKB pathway.

Indexed as

Cell CycleProtein Serine-Threonine KinasesTumor Suppressor Proteins3T3 CellsAnimalsBiological TransportCytosolG1 PhaseGlioblastomaHeLa CellsHumansMiceMutagenesisPhosphatidylinositol-3,4,5-Trisphosphate 5-PhosphatasesPhosphatidylinositol PhosphatesPhosphoprotein PhosphatasesINPPL1 protein, humanphosphatidylinositol 3,4,5-triphosphatePhosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatasesphosphatidylinositol 3,4-diphosphatePhosphatidylinositol PhosphatesPhosphoprotein PhosphatasesPhosphoric Monoester HydrolasesProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktPTEN PhosphohydrolasePTEN protein, humanTumor Suppressor ProteinsTyrosine

Identifiers

PMID10958682
PMCPMC86225
OpenAlexW2154365640

What Socratic 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 Socratic graph.