Phosphatidylinositol 5-phosphate regulates invasion through binding and activation of Tiam1

Julien Viaud, Frédéric Lagarrigue, Damien Ramel, Sophie Allart, Gaëtan Chicanne, Laurie Ceccato, Delphine Courilleau, Jean-Marie Xuereb, Olivier Pertz, Bernard Payrastre and Frédérique Gaits-Iacovoni ()
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Julien Viaud: INSERM, UMR1048, Université Toulouse III, Institut des Maladies Métaboliques et Cardiovasculaires
Frédéric Lagarrigue: INSERM, UMR1048, Université Toulouse III, Institut des Maladies Métaboliques et Cardiovasculaires
Damien Ramel: INSERM, UMR1048, Université Toulouse III, Institut des Maladies Métaboliques et Cardiovasculaires
Sophie Allart: INSERM, UMR1043, Plateau Technique D'imagerie Cellulaire, Centre de Physiopathologie de Toulouse Purpan
Gaëtan Chicanne: INSERM, UMR1048, Université Toulouse III, Institut des Maladies Métaboliques et Cardiovasculaires
Laurie Ceccato: INSERM, UMR1048, Université Toulouse III, Institut des Maladies Métaboliques et Cardiovasculaires
Delphine Courilleau: INSERM, UMR1048, Université Toulouse III, Institut des Maladies Métaboliques et Cardiovasculaires
Jean-Marie Xuereb: INSERM, UMR1048, Université Toulouse III, Institut des Maladies Métaboliques et Cardiovasculaires
Olivier Pertz: Institute of Biochemistry and Genetics, University of Basel
Bernard Payrastre: INSERM, UMR1048, Université Toulouse III, Institut des Maladies Métaboliques et Cardiovasculaires
Frédérique Gaits-Iacovoni: INSERM, UMR1048, Université Toulouse III, Institut des Maladies Métaboliques et Cardiovasculaires

Nature Communications, 2014, vol. 5, issue 1, 1-17

Abstract: Abstract PtdIns5P is a lipid messenger acting as a stress-response mediator in the nucleus, and known to maintain cell activation through traffic alterations upon bacterial infection. Here, we show that PtdIns5P regulates actin dynamics and invasion via recruitment and activation of the exchange factor Tiam1 and Rac1. Restricted Rac1 activation results from the binding of Tiam1 DH-PH domains to PtdIns5P. Using an assay that mimics Rac1 membrane anchoring by using Rac1-His and liposomes containing Ni2+-NTA modified lipids, we demonstrate that intrinsic Tiam1 DH-PH activity increases when Rac1 is anchored in a PtdIns5P-enriched environment. This pathway appears to be general since it is valid in different pathophysiological models: receptor tyrosine kinase activation, bacterial phosphatase IpgD expression and the invasive NPM-ALK(+) lymphomas. The discovery that PtdIns5P could be a keystone of GTPases and cytoskeleton spatiotemporal regulation opens important research avenues towards unravelling new strategies counteracting cell invasion.

Date: 2014
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DOI: 10.1038/ncomms5080

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