The PX domains of p47phox and p40phox bind to lipid products of PI(3)K

By F. Kanai, Hui Liu, S. Field, Hares Akbary, T. Matsuo, G. Brown, Lewis C. Cantley, Michael B. Yaffe. Nature Cell Biology, 2001

646 citations recorded by the source corpus.

Subfields: Cell Biology, Immunology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/b0e46f5ce2e84cefbcacad5627c811341570443a

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Citations in the corpus

• The endocytic pathway: a mosaic of domains (2001, background): “This was first found in p40 phox and p47 phox — two subunits of the neutrophil oxidas”
• Regulation of reactive oxygen species generation in cell signaling (2011, background): “PX domain in p40 can specifically bind to phosphatidylinositol 3-phosphate [PI(3)P], highly enriched in the phagosomal membrane (Bravo et al., 2001; Kanai et al., 2001; Stahelin et al., 2003).”
• PI3K signalling: the path to discovery and understanding (2012, background): “This was followed in 2001 by the identification of the phox (PX) domain as a PtdIns(3)P-binding module in various proteins, including many involved in vesicular transpor”
• Phosphoinositides: tiny lipids with giant impact on cell regulation. (2013, background): “Accordingly, PtdIns3P exerts its effects by recruiting a variety of proteins that contain PI binding domains that are attracted to the membrane by this particular PPI species.”
• LAMP proteins are required for fusion of lysosomes with phagosomes (2007, methodology): “The p40phox-PX domain vector (Kanai et al, 2001) was provided by Dr M Yaffe (MIT, Cambridge, MA).”
• Sorting out the cellular functions of sorting nexins (2002, background): “The hallmark of this protein family is the presence of a PX DOMAIN — a sequence of approximately 100–130 amino acids that has recently been shown to bind various phosphatidylinositol phosphates (PtdInsPs), thereby potentially targeting these proteins to specific cellular membranes that are enriche”
• International Union of Basic and Clinical Pharmacology. LXXIII. Nomenclature for the Formyl Peptide Receptor (FPR) Family (2009, background): “The degradation products of PtdIns(3,4,5)P3, including phosphatidylinositol (3,4)- bisphosphate and phosphatidylinositol phosphate, serve as membrane binding sites for the PX domain of p47phox and p40phox, respectively (Kanai et al., 2001).”
• Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking (2008, background): “Epitope-tagged Vps16, Vps18, Vps11 and Vps33 showed punctate staining and extensive colocalization with EEA1 and p40(phox)PX–GFP, a probe for phosphatidylinositol-3-phosphate (PtdIns(3)P)-enriched early endosome”
• Neutrophils to the ROScue: Mechanisms of NADPH Oxidase Activation and Bacterial Resistance (2017, background): “This further exposes the binding pocket for p22phox, brings p67phox and p40phox in proximity of cytb558, and allows PX domain to bind to PtdIns(3,4)P2 and phosphatidic acid (Shiose and Sumimoto, 2000; Kanai et al., 2001; Bokoch et al., 2009; El-Benna et al., 2009; Li et al., 2010; Meijles et al., 20”
• Combating oxidative stress in vascular disease: NADPH oxidases as therapeutic targets (2011, background): “Detailed mutagenesis studies and X-ray crystallography of the p47phox PX domain have revealed that it also contains two highly basic pockets that bind to membrane phosphoinositides following unfolding of the protei”