title: Signaling by distinct classes of phosphoinositide 3-kinases.
abstract: Many signaling pathways converge on and regulate phosphoinositide 3-kinase (PI3K) enzymes whose inositol lipid products are key mediators of intracellular signaling. Different PI3K isoforms generate specific lipids that bind to FYVE and pleckstrin homology (PH) domains in a variety of proteins, affecting their localization, conformation, and activities. Here we review the activation mechanisms of the different types of PI3Ks and their downstream actions, with focus on the PI3Ks that are acutely triggered by extracellular stimulation.
authors.affiliation: Ludwig Institute for Cancer Research, 91 Riding House Street, London, W1P 8BT, United Kingdom. bartvanh@ludwig.ucl.ac.uk
authors.forename: B
authors.initials: B
authors.lastname: Vanhaesebroeck
authors.forename: M D
authors.initials: MD
authors.lastname: Waterfield
mesh_terms: D000818:Animals; D001665:Binding Sites; D007527:Isoenzymes / Q000037:antagonists & inhibitors / Q000145:classification / Q000378:metabolism; D051379:Mice; D018345:Mice, Knockout; D019869:Phosphatidylinositol 3-Kinases / Q000145:classification* / Q000235:genetics / Q000378:metabolism*; D000081082:Phosphoinositide-3 Kinase Inhibitors; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D017434:Protein Structure, Tertiary; D015398:Signal Transduction
chemical_list: D007527:Isoenzymes; D019869:Phosphatidylinositol 3-Kinases; D000081082:Phosphoinositide-3 Kinase Inhibitors; D017346:Protein Serine-Threonine Kinases