TOM1 is a PI5P effector involved in the regulation of endosomal maturation

Phosphoinositides represent a major class of lipids specifically involved in the organization of signaling cascades, maintenance of the identity of organelles and regulation of multiple intracellular trafficking steps. We previously reported that phosphatidylinositol 5-monophosphate (PI5P), produced...

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Bibliographic Details
Published in:	Journal of cell science Vol. 128; no. 4; pp. 815 - 827
Main Authors:	Boal, Frédéric, Mansour, Rana, Gayral, Marion, Saland, Estelle, Chicanne, Gaëtan, Xuereb, Jean-Marie, Marcellin, Marlène, Burlet-Schiltz, Odile, Sansonetti, Philippe J, Payrastre, Bernard, Tronchère, Hélène
Format:	Journal Article
Language:	English
Published:	England 15-02-2015
Subjects:	Animals Binding Sites Cell Line Cloning, Molecular Cricetinae Endocytosis - genetics Endocytosis - physiology Endosomes - metabolism Fibroblasts HeLa Cells Humans Mice Mutagenesis, Site-Directed Phosphatidylinositol Phosphates - metabolism Protein Binding Protein Structure, Tertiary Protein Transport Proteins - genetics Proteins - metabolism Receptor, Epidermal Growth Factor - metabolism RNA Interference RNA, Small Interfering Signal Transduction TOM1 Signaling endosome Phosphoinositides VHS domain EGFR
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Summary:	Phosphoinositides represent a major class of lipids specifically involved in the organization of signaling cascades, maintenance of the identity of organelles and regulation of multiple intracellular trafficking steps. We previously reported that phosphatidylinositol 5-monophosphate (PI5P), produced by the Shigella flexneri phosphatase IpgD, is implicated in the endosomal sorting of the epidermal growth factor receptor (EGFR). Here, we show that the adaptor protein TOM1 is a new direct binding partner of PI5P. We identify the domain of TOM1 involved in this interaction and characterize the binding motif. Finally, we demonstrate that the recruitment of TOM1 by PI5P on signaling endosomes is responsible for the delay in EGFR degradation and fluid-phase bulk endocytosis. Taken together, our data strongly suggest that PI5P enrichment in signaling endosomes prevents endosomal maturation through the recruitment of TOM1, and point to a new function of PI5P in regulating discrete maturation steps in the endosomal system.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0021-9533 1477-9137
DOI:	10.1242/jcs.166314