Evidence map›Paper›PMID 26596865›Full record

ArticleAdvances in biological regulation2016

Localizing the lipid products of PI3Kγ in neutrophils.

Laura Norton, Yvonne Lindsay, Arnaud Deladeriere, Tamara Chessa, Hervé Guillou, Sabine Suire, John Lucocq, Simon Walker, Simon Andrews, Anne Segonds-Pichon and 8 more

Open access · hybridAbstract read
In one paragraph

Article in Advances in biological regulation, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

7 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Rac-GTPases and Rac-GEFs in neutrophil adhesion, migration and recruitment.European journal of clinical investigation · 2018
    Review
  7. 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

18 authors at 7 institutions in 7 countries.

Laura NortonThe Signalling Department, The Babraham Institute, The Babraham Research Campus, Cambridge, CB22 3AT, United Kingdom.
Yvonne LindsayDivision of Molecular Physiology, College of Life Sciences, University of Dundee, Dundee, DD1 5EH, UK; Division of Cell Biology and Immunology, College of Life Sciences, University of Dundee, Dundee, DD1 5EH, UK.
Arnaud DeladeriereThe Signalling Department, The Babraham Institute, The Babraham Research Campus, Cambridge, CB22 3AT, United Kingdom.
Tamara ChessaThe Signalling Department, The Babraham Institute, The Babraham Research Campus, Cambridge, CB22 3AT, United Kingdom.
Hervé GuillouLaboratoire de Pharmacologie et Toxicologie, INRA UR66, Toulouse, France.
Sabine SuireThe Signalling Department, The Babraham Institute, The Babraham Research Campus, Cambridge, CB22 3AT, United Kingdom.
John LucocqDivision of Cell Biology and Immunology, College of Life Sciences, University of Dundee, Dundee, DD1 5EH, UK.
Simon WalkerThe Imaging Facility, The Babraham Institute, The Babraham Research Campus, Cambridge, CB22 3AT, UK.
Simon AndrewsThe Bioinformatics Group, The Babraham Institute, The Babraham Research Campus, Cambridge, CB22 3AT, UK.
Anne Segonds-PichonThe Bioinformatics Group, The Babraham Institute, The Babraham Research Campus, Cambridge, CB22 3AT, UK.
Oliver RauschUCB, Allée de la Recherche, 60 1070 Brussels, Belgium.
Peter FinanDevelopmental and Molecular Pathways, Novartis Institutes for BioMedical Research, 250 Massachusetts Avenue, Cambridge, MA 02139, USA.
Takehiko SasakiDepartment of Pathology and Immunology, Akita University School of Medicine, 1-1-1 Hondo, Akita 010-8543, Japan.
Cheng-Jin DuWarwick Systems Biology Centre, University of Warwick, UK.
Till BretschneiderWarwick Systems Biology Centre, University of Warwick, UK.
G John FergusonThe Signalling Department, The Babraham Institute, The Babraham Research Campus, Cambridge, CB22 3AT, United Kingdom.
Phillip T HawkinsThe Signalling Department, The Babraham Institute, The Babraham Research Campus, Cambridge, CB22 3AT, United Kingdom.
Len StephensThe Signalling Department, The Babraham Institute, The Babraham Research Campus, Cambridge, CB22 3AT, United Kingdom. Electronic address: len.stephens@bbsrc.ac.uk.
Babraham Institute · GBUniversity of Dundee · GBUniversity of Warwick · GBAkita University · JPNovartis (Switzerland) · CHToxicologie Alimentaire · FRUCB Pharma (Belgium) · BE

Funding

Biotechnology and Biological Sciences Research Council 8443Biotechnology and Biological Sciences Research Council BB/B511900/1Biotechnology and Biological Sciences Research Council BB/B5119001/1Biotechnology and Biological Sciences Research Council BB/D013593/1Biotechnology and Biological Sciences Research Council BB/I008209/1Biotechnology and Biological Sciences Research Council BBS/E/B/000C0411Biotechnology and Biological Sciences Research Council C20177Medical Research Council MR/K018167/1
6 · The paper itself

Abstract

Class I phosphoinositide 3-kinases (PI3Ks) are important regulators of neutrophil migration in response to a range of chemoattractants. Their primary lipid products PtdIns(3,4,5)P3 and PtdIns(3,4)P2 preferentially accumulate near to the leading edge of migrating cells and are thought to act as an important cue organizing molecular and morphological polarization. We have investigated the distribution and accumulation of these lipids independently in mouse neutrophils using eGFP-PH reportersand electron microscopy (EM). We found that authentic mouse neutrophils rapidly polarized their Class I PI3K signalling, as read-out by eGFP-PH reporters, both at the up-gradient leading edge in response to local stimulation with fMLP as well as spontaneously and randomly in response to uniform stimulation. EM studies revealed these events occurred at the plasma membrane, were dominated by accumulation of PtdIns(3,4,5)P3, but not PtdIns(3,4)P2, and were dependent on PI3Kγ and its upstream activation by both Ras and Gβγs.

Indexed as

AnimalsCells, CulturedClass Ib Phosphatidylinositol 3-KinaseMiceNeutrophilsPhosphatidylinositol PhosphatesProtein TransportClass Ib Phosphatidylinositol 3-Kinasephosphatidylinositol 3,4,5-triphosphatephosphatidylinositol 3,4-diphosphatePhosphatidylinositol PhosphatesPik3cg protein, mouseNeutrophilPI3KPolarization

Identifiers

PMID26596865
PMCPMC4739120
OpenAlexW2176717776

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.