Evidence map›Paper›PMID 24485835›Full record

ArticleCurrent biology : CB2014

A PIP5 kinase essential for efficient chemotactic signaling.

Louise Fets, John M E Nichols, Robert R Kay

Open access · hybridAbstract read
In one paragraph

Article in Current biology : CB, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

24 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. The Amoebal Model for Macropinocytosis.Sub-cellular biochemistry · 2022
    Article
  3. Gradients of PI(4,5)PFrontiers in cell and developmental biology · 2022
    Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. The origins and evolution of macropinocytosis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. IQGAP1 is a phosphoinositide effector and kinase scaffold.Advances in biological regulation · 2016
    Review
  19. Review
  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

3 authors at 1 institution in 1 country.

Louise FetsCell Biology Division, MRC Laboratory of Molecular Biology, Cambridge Biomedical Campus, Francis Crick Avenue, Cambridge CB2 0QH, UK. Electronic address: lfets@nimr.mrc.ac.uk.
John M E NicholsCell Biology Division, MRC Laboratory of Molecular Biology, Cambridge Biomedical Campus, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Robert R KayCell Biology Division, MRC Laboratory of Molecular Biology, Cambridge Biomedical Campus, Francis Crick Avenue, Cambridge CB2 0QH, UK.
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105115237Medical Research Council U105115237
6 · The paper itself

Abstract

In neutrophils and Dictyostelium, chemoattractant gradients generate directed cell migration by eliciting signaling events that bias intrinsic motility and favor the production and retention of upgradient pseudopods. Phosphoinositides are actively regulated during chemotaxis in these cells, most iconically in the production of PI(3,4,5)P3 gradients within the plasma membrane. Although it is now known that PI(3,4,5)P3 signaling is nonessential for gradient sensing, the role of the related phosphoinositide PI(4,5)P2 is little understood, despite its clear importance in many cell biological processes. We describe here a PIP5 kinase, PikI, which produces PI(4,5)P2 and is essential for efficient chemotaxis of Dictyostelium cells. Without PikI, PI(4,5)P2 levels are reduced by 90%, and while pikI(-) cells move at normal speeds, they are highly disorientated in cAMP gradients. Following chemotactic stimulation, Ras is efficiently activated in pikI(-) cells, yet Ras-dependent responses (including activation of PKB) are severely impaired. PikI is phosphorylated by PKB, and in vitro studies of a phosphomimic mutant suggest that this phosphorylation increases PikI activity. We propose that adequate PI(4,5)P2 levels are required to couple activated Ras to its downstream effectors and that these levels are regulated by PikI, making it a crucial player in gradient sensing.

Indexed as

ChemotaxisSignal TransductionCyclic AMPDictyosteliumEnzyme ActivationPhosphorylationPhosphotransferases (Alcohol Group Acceptor)Proto-Oncogene Proteins c-akt1-phosphatidylinositol-4-phosphate 5-kinaseCyclic AMPPhosphotransferases (Alcohol Group Acceptor)Proto-Oncogene Proteins c-akt

Identifiers

PMID24485835
PMCPMC3969243
OpenAlexW2008682878

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.