title: Phosphoinositides influence pathogen surfing: EPEC rights the SHIP.
abstract: Tir, a translocated effector protein from enteropathogenic E. coli (EPEC), contains two phosphotyrosines that initiate cellular signaling cascades, leading to localized actin polymerization into pedestals. A recent study now shows that two additional tyrosines within Tir recruit the inositol phosphatase SHIP2 to generate a PI(3,4)P2-enriched membrane platform that stabilizes pedestal assembly.
authors.affiliation: Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA. campellone@berkeley.edu
authors.forename: Kenneth G
authors.initials: KG
authors.lastname: Campellone
mesh_terms: D000199:Actins / Q000378:metabolism*; D054308:Enteropathogenic Escherichia coli / Q000472:pathogenicity*; D029968:Escherichia coli Proteins / Q000502:physiology*; D008954:Models, Biological; D000072183:Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases; D010716:Phosphatidylinositols / Q000378:metabolism; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D011485:Protein Binding; D011956:Receptors, Cell Surface / Q000502:physiology*; D015398:Signal Transduction; D037521:Virulence Factors / Q000502:physiology*
chemical_list: D000199:Actins; D029968:Escherichia coli Proteins; D010716:Phosphatidylinositols; D011956:Receptors, Cell Surface; C109287:Tir protein, E coli; D037521:Virulence Factors; D010744:Phosphoric Monoester Hydrolases; C098706:INPPL1 protein, human; D000072183:Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases