Evidence map›Paper›PMID 17442886›Full record

ArticleMolecular biology of the cell2007

Differential association of phosphatidylinositol 3-kinase, SHIP-1, and PTEN with forming phagosomes.

Lynn A Kamen, Jonathan Levinsohn, Joel A Swanson

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2007. 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
3.4field-weighted citation impact, top 7% 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, 79 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Genome-wide studies define new genetic mechanisms of IgA vasculitis.medRxiv : the preprint server for health sciences · 2024
    Article
  5. Article
  6. Targeting Microglia-Synapse Interactions in Alzheimer's Disease.International journal of molecular sciences · 2021
    Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Microglia in Alzheimer's disease.The Journal of cell biology · 2018
    Review
  17. Review
  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

3 authors at 2 institutions in 2 countries.

Lynn A KamenDepartment of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI 48109-0620, USA.
Jonathan Levinsohn
Joel A Swanson
University of Michigan · USBipar · FR

Funding

MANIPULATION OF PHAGOCYTOSIS IN MACROPHAGESR01AI035950 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SWANSON, JOEL A · 1994 to 2008
$2.2M
Coordination of signaling during phagocytosisR01AI064668 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SWANSON, JOEL A · 2005 to 2010
$1.6M
MANIPULATION OF PHAGOCYTOSIS IN MACROPHAGESR21AI035950 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SWANSON, JOEL A · 1999 to 1999
–
NIAID NIH HHS AI-35950NIAID NIH HHS AI-64668NIAID NIH HHS R01 AI035950NIAID NIH HHS R01 AI064668NIAID NIH HHS R21 AI035950
6 · The paper itself

Abstract

In macrophages, enzymes that synthesize or hydrolyze phosphatidylinositol (3,4,5)-trisphosphate [PI(3,4,5)P(3)] regulate Fcgamma receptor-mediated phagocytosis. Inhibition of phosphatidylinositol 3-kinase (PI3K) or overexpression of the lipid phosphatases phosphatase and tensin homologue (PTEN) and Src homology 2 domain-containing inositol phosphatase (SHIP-1), which hydrolyze PI(3,4,5)P(3) to phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4-bisphosphate [PI(3,4)P(2)], respectively, inhibit phagocytosis in macrophages. To examine how these enzymes regulate phagosome formation, the distributions of yellow fluorescent protein (YFP) chimeras of enzymes and pleckstrin homology (PH) domains specific for their substrates and products were analyzed quantitatively. PTEN-YFP did not localize to phagosomes, suggesting that PTEN regulates phagocytosis globally within the macrophage. SHIP1-YFP and p85-YFP were recruited to forming phagosomes. SHIP1-YFP sequestered to the leading edge and dissociated from phagocytic cups earlier than did p85-cyan fluorescent protein, indicating that SHIP-1 inhibitory activities are restricted to the early stages of phagocytosis. PH domain chimeras indicated that early during phagocytosis, PI(3,4,5)P(3) was slightly more abundant than PI(3,4)P(2) at the leading edge of the forming cup. These results support a model in which phagosomal PI3K generates PI(3,4,5)P(3) necessary for later stages of phagocytosis, PTEN determines whether those late stages can occur, and SHIP-1 regulates when and where they occur by transiently suppressing PI(3,4,5)P(3)-dependent activities necessary for completion of phagocytosis.

Indexed as

AnimalsCell LineHumansInositol Polyphosphate 5-PhosphatasesMiceMicroscopy, FluorescenceModels, BiologicalPhagocytosisPhagosomesPhosphatidylinositol-3,4,5-Trisphosphate 5-PhosphatasesPhosphatidylinositol 3-KinasesPhosphatidylinositolsPhosphoric Monoester HydrolasesProtein Structure, TertiaryProtein TransportPTEN PhosphohydrolaseInositol Polyphosphate 5-PhosphatasesINPP5D protein, humanInpp5d protein, mousePhosphatidylinositol-3,4,5-Trisphosphate 5-PhosphatasesPhosphatidylinositol 3-KinasesPhosphatidylinositolsPhosphoric Monoester HydrolasesPTEN PhosphohydrolasePten protein, mouseRecombinant Fusion Proteins

Identifiers

PMID17442886
PMCPMC1924803
OpenAlexW2149766306

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.