Localizing the lipid products of PI3Kγ in neutrophils

Autor: Arnaud Deladeriere, Hervé Guillou, Sabine Suire, Oliver Rausch, G. John Ferguson, Simon Andrews, Simon Walker, Tamara Chessa, Till Bretschneider, Cheng-Jin Du, Laura J. Norton, Anne Segonds-Pichon, Len R. Stephens, Takehiko Sasaki, Peter Finan, Yvonne E. Lindsay, Phillip T. Hawkins, John M. Lucocq
Přispěvatelé: Signalling Department, Babraham Institute, College of Life Sciences, Division of Molecular Physiology, University of Dundee, College of Life Sciences, Division of Cell Biology and Immunology, Toxicologie Intégrative & Métabolisme (ToxAlim-TIM), ToxAlim (ToxAlim), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Ecole Nationale Vétérinaire de Toulouse (ENVT), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Ecole d'Ingénieurs de Purpan (INPT - EI Purpan), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Recherche Agronomique (INRA)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Recherche Agronomique (INRA), The Imaging Facility, Bioinformatics Group, Wageningen University, UCB, Novartis Institutes for BioMedical Research (NIBR), School of Medicine, University of Patras [Greece], Warwick Systems Biology Centre, University of Warwick, Stephens, Len, University of St Andrews. School of Medicine, University of St Andrews. Biomedical Sciences Research Complex
Rok vydání: 2016
Předmět:
0301 basic medicine
Cancer Research
phosphoinositide 3 kinase
neutrophile
Neutrophils
QH301 Biology
[SDV]Life Sciences [q-bio]
Stimulation
PI3K
Green fluorescent protein
Mice
PH
Pleckstrin homology
Phosphatidylinositol Phosphates
Polarization
PI3K
Phosphoinositide 3-kinase
Class Ib Phosphatidylinositol 3-Kinase
Cells
Cultured
fMLP
formylated-Met-Leu-Phe
biology
Neutrophil
TAPP-1
TAndem PH domain containing Protein-1
neutrophil
microscopie électronique
Cell biology
Transport protein
Protein Transport
Biochemistry
Molecular Medicine
polarization
GPCR
G-Protein Coupled Receptor
NDAS
polarisation
R Medicine
eGFP
enhanced Green Fluorescent Protein
Article
QH301
03 medical and health sciences
Genetics
Animals
Molecular Biology
PI3K/AKT/mTOR pathway
G protein-coupled receptor
EM
Electron Microscopy
Phosphoinositide 3-kinase
electron microscopy
Chemotaxis
030104 developmental biology
PKB
Protein Kinase B (also called Akt)
biology.protein
Zdroj: Advances in Biological Regulation
Advances in Biological Regulation, 2016, 60, pp.36-45. ⟨10.1016/j.jbior.2015.10.005⟩
Advances in Biological Regulation (60), 36-45. (2016)
ISSN: 2212-4926
DOI: 10.1016/j.jbior.2015.10.005
Popis: 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 reporters and 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. Publisher PDF
Databáze: OpenAIRE
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