Evidence map›Paper›PMID 11352940›Full record

ArticleThe Journal of cell biology2001

Role of phosphatidylinositol 3' kinase and a downstream pleckstrin homology domain-containing protein in controlling chemotaxis in dictyostelium.

S Funamoto, K Milan, R Meili, R A Firtel

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
106citing papers in PubMed, 1 pooled it
6.6field-weighted citation impact, top 3% 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

106 citing papers in PubMed, 1 synthesis or guideline pooled it, 227 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Gradients of PI(4,5)PFrontiers in cell and developmental biology · 2022
    Article
  6. Article
  7. From environmental sensing to developmental control: cognitive evolution in dictyostelid social amoebas.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2021
    Article
  8. Ras, PI3K and mTORC2 - three's a crowd?Journal of cell science · 2020
    Review
  9. Single-molecule imaging of PI(4,5)PCommunications biology · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Collective cell migration ofCommunications biology · 2019
    Article
  15. Article
  16. Article
  17. Function and Regulation of Heterotrimeric G Proteins during Chemotaxis.International journal of molecular sciences · 2016
    Review
  18. Article
  19. Article
  20. Article

46 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

S FunamotoSection of Cell and Developmental Biology and Center for Molecular Genetics, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.
K Milan
R Meili
R A Firtel
University of California, San Diego · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We show that cells lacking two Dictyostelium class I phosphatidylinositol (PI) 3' kinases (PI3K and pi3k1/2-null cells) or wild-type cells treated with the PI3K inhibitor LY294002 are unable to properly polarize, are very defective in the temporal, spatial, and quantitative regulation of chemoattractant-mediated filamentous (F)-actin polymerization, and chemotax very slowly. PI3K is thought to produce membrane lipid-binding sites for localization of PH domain-containing proteins. We demonstrate that in response to chemoattractants three PH domain-containing proteins do not localize to the leading edge in pi3k1/2-null cells, and the translocation is blocked in wild-type cells by LY294002. Cells lacking one of these proteins, phdA-null cells, exhibit defects in the level and kinetics of actin polymerization at the leading edge and have chemotaxis phenotypes that are distinct from those described previously for protein kinase B (PKB) (pkbA)-null cells. Phenotypes of PhdA-dominant interfering mutations suggest that PhdA is an adaptor protein that regulates F-actin localization in response to chemoattractants and links PI3K to the control of F-actin polymerization at the leading edge during pseudopod formation. We suggest that PKB and PhdA lie downstream from PI3K and control different downstream effector pathways that are essential for proper chemotaxis.

Indexed as

Protein Serine-Threonine KinasesActinsAmino Acid SequenceAnimalsBlood ProteinsChemotaxisChromonesDictyosteliumEnzyme InhibitorsFolic AcidKineticsMicroscopy, VideoMolecular Sequence DataMorpholinesMutagenesis, InsertionalPhosphatidylinositol 3-Kinases2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-oneActinsBlood ProteinsChromonesEnzyme InhibitorsFolic AcidMorpholinesPhdA protein, DictyosteliumPhosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase InhibitorsPhosphoproteinsplatelet protein P47PolymersProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktProtozoan Proteins

Identifiers

PMID11352940
PMCPMC2192389
OpenAlexW2123332655

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.