Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
The PX domains of p47phox and p40phox bind to lipid products of Pl(3)K
Autore:
Kanai, F; Liu, H; Field, SJ; Akbary, H; Matsuo, T; Brown, GE; Cantley, LC; Yaffe, MB;
Indirizzi:
MIT, Ctr Canc Res, Cambridge, MA 02139 USA MIT Cambridge MA USA 02139MIT, Ctr Canc Res, Cambridge, MA 02139 USA MIT, Dept Biol, Cambridge, MA 02139 USA MIT Cambridge MA USA 02139MIT, Dept Biol, Cambridge, MA 02139 USA Harvard Univ, Sch Med, Beth Israel Deaconess Med Ctr, Div Signal Transduct, Boston, MA 02215 USA Harvard Univ Boston MA USA 02215 v Signal Transduct, Boston, MA 02215 USA Harvard Univ, Sch Med, Dept Cell Biol, Boston, MA 02215 USA Harvard Univ Boston MA USA 02215 ed, Dept Cell Biol, Boston, MA 02215 USA Massachusetts Gen Hosp, Div Endocrinol, Boston, MA 02114 USA MassachusettsGen Hosp Boston MA USA 02114 docrinol, Boston, MA 02114 USA Beth Israel Deaconess Med Ctr, Dept Surg, Boston, MA 02215 USA Beth IsraelDeaconess Med Ctr Boston MA USA 02215 g, Boston, MA 02215 USA
Titolo Testata:
NATURE CELL BIOLOGY
fascicolo: 7, volume: 3, anno: 2001,
pagine: 675 - 678
SICI:
1465-7392(200107)3:7<675:TPDOPA>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHOSPHATIDYLINOSITOL 3-KINASE; PHOSPHOINOSITIDE-BINDING; NADPH OXIDASE; ENDOSOMAL LOCALIZATION; HOMOLOGY DOMAINS; SORTING NEXIN; IDENTIFICATION; 3-PHOSPHATE; PLECKSTRIN; RECEPTORS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Yaffe, MB MIT, Ctr Canc Res, 77 Massachusetts Ave, Cambridge, MA 02139 USAMIT 77 Massachusetts Ave Cambridge MA USA 02139 ge, MA 02139 USA
Citazione:
F. Kanai et al., "The PX domains of p47phox and p40phox bind to lipid products of Pl(3)K", NAT CELL BI, 3(7), 2001, pp. 675-678

Abstract

PX domains are found in a variety of proteins that associate with cell membranes, but their molecular function has remained obscure. We show here that the PX domains in p47phox and p40phox subunits of the phagocyte NADPH oxidase bind to phosphatidylinositol-3,4-bisphosphate (Ptdlns(3,4)P-2) and phosphatidylinositol-3-phosphate (Ptdlns(3)P), respectively. We also show thatan Arg-to-Gln mutation in the PX domain of p47phox, which is found in patients with chronic granulomatous disease, eliminates phosphoinositide binding, as does the analogous mutation in the PX domain of p40phox, The PX domain of p40phox localizes specifically to Ptdlns(B)P-enriched early endosomes,and this localization is disrupted by inhibition of phosphoinositide-3-OH kinase (PI(3)K) or by the Arg-to-Gln point mutation. These findings providea molecular foundation to understand the role of PI(3)K in regulating neutrophil function and inflammation, and to identify PX domains as specific phosphoinositide-binding modules involved in signal transduction events in eukaryotic cells.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/03/20 alle ore 23:19:27