Evidence map›Paper›PMID 15716355›Full record

ArticleMolecular biology of the cell2005

The type Ialpha inositol polyphosphate 4-phosphatase generates and terminates phosphoinositide 3-kinase signals on endosomes and the plasma membrane.

Ivan Ivetac, Adam D Munday, Marina V Kisseleva, Xiang-Ming Zhang, Susan Luff, Tony Tiganis, James C Whisstock, Tony Rowe, Phillip W Majerus, Christina A Mitchell

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
3.4field-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

54 citing papers in PubMed, 101 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Lipid-dependent Akt-ivity: where, when, and how.Biochemical Society transactions · 2019
    Review
  14. Secretory Inositol Polyphosphate 4-Phosphatase Protects against Airway Inflammation and Remodeling.American journal of respiratory cell and molecular biology · 2019
    Article
  15. Article
  16. Phosphatidylinositol Kinases and Phosphatases inFrontiers in cellular and infection microbiology · 2019
    Review
  17. Article
  18. Article
  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

10 authors at 2 institutions in 2 countries.

Ivan IvetacDepartment of Biochemistry and Molecular Biology, Monash University, Clayton, Australia 3800.
Adam D Munday
Marina V Kisseleva
Xiang-Ming Zhang
Susan Luff
Tony Tiganis
James C Whisstock
Tony Rowe
Phillip W Majerus
Christina A Mitchell
Monash University · AUWashington University in St. Louis · US

Funding

The Role of Inositol Signaling in Human DiseaseR01HL055672 · NHLBI · WASHINGTON UNIVERSITY · PI YORK, JOHN D. · 1996 to 2012
$5.4M
NHLBI NIH HHS HL-55672NHLBI NIH HHS R01 HL055672
6 · The paper itself

Abstract

Endosomal trafficking is regulated by the recruitment of effector proteins to phosphatidylinositol 3-phosphate [PtdIns(3)P] on early endosomes. At the plasma membrane, phosphatidylinositol-(3,4)-bisphosphate [PtdIns(3,4)P2] binds the pleckstrin homology (PH) domain-containing proteins Akt and TAPP1. Type Ialpha inositol polyphosphate 4-phosphatase (4-phosphatase) dephosphorylates PtdIns(3,4)P2, forming PtdIns(3)P, but its subcellular localization is unknown. We report here in quiescent cells, the 4-phosphatase colocalized with early and recycling endosomes. On growth factor stimulation, 4-phosphatase endosomal localization persisted, but in addition the 4-phosphatase localized at the plasma membrane. Overexpression of the 4-phosphatase in serum-stimulated cells increased cellular PtdIns(3)P levels and prevented wortmannin-induced endosomal dilatation. Furthermore, mouse embryonic fibroblasts from homozygous Weeble mice, which have a mutation in the type I 4-phosphatase, exhibited dilated early endosomes. 4-Phosphatase translocation to the plasma membrane upon growth factor stimulation inhibited the recruitment of the TAPP1 PH domain. The 4-phosphatase contains C2 domains, which bound PtdIns(3,4)P2, and C2-domain-deletion mutants lost PtdIns(3,4)P2 4-phosphatase activity, did not localize to endosomes or inhibit TAPP1 PH domain membrane recruitment. The 4-phosphatase therefore both generates and terminates phosphoinositide 3-kinase signals at distinct subcellular locations.

Indexed as

AndrostadienesAnimalsBiological Transport, ActiveCell MembraneCells, CulturedChlorocebus aethiopsCHO CellsCOS CellsCricetinaeEndosomesEpidermal Growth FactorHumansIntracellular Signaling Peptides and ProteinsIn Vitro TechniquesMembrane ProteinsMiceAKT1 protein, humanAndrostadienesEpidermal Growth FactorIntracellular Signaling Peptides and ProteinsMembrane Proteinsphosphatidylinositol-3,4-bisphosphate 4-phosphatasePhosphatidylinositol 3-Kinasesphosphatidylinositol 3-phosphatePhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol PhosphatesPhosphoric Monoester HydrolasesPLEKHA1 protein, humanProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktrab GTP-Binding ProteinsRecombinant ProteinsWortmannin

Identifiers

PMID15716355
PMCPMC1087230
OpenAlexW2163669083

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.