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Titolo:
Enteropathogenic E-coli Tir binds Nck to initiate actin pedestal formationin host cells
Autore:
Gruenheid, S; DeVinney, R; Bladt, F; Goosney, D; Gelkop, S; Gish, GD; Pawson, T; Finlay, BB;
Indirizzi:
Univ British Columbia, Biotechnol Lab, Vancouver, BC V6T 1G3, Canada Univ British Columbia Vancouver BC Canada V6T 1G3 ver, BC V6T 1G3, Canada Mt Sinai Hosp, Program Mol Biol & Canc, Samuel Lunenfeld Res Inst, Toronto, ON M5G 1X5, Canada Mt Sinai Hosp Toronto ON Canada M5G 1X5 Inst, Toronto, ON M5G 1X5, Canada
Titolo Testata:
NATURE CELL BIOLOGY
fascicolo: 9, volume: 3, anno: 2001,
pagine: 856 - 859
SICI:
1465-7392(200109)3:9<856:EETBNT>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSLOCATED INTIMIN RECEPTOR; ADAPTER PROTEIN; POLYMERIZATION; COMPLEX; WASP;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Finlay, BB Univ British Columbia, Biotechnol Lab, 6174 Univ Blvd, Vancouver, BC V6T 1G3, Canada Univ British Columbia 6174 Univ Blvd Vancouver BC Canada V6T 1G3
Citazione:
S. Gruenheid et al., "Enteropathogenic E-coli Tir binds Nck to initiate actin pedestal formationin host cells", NAT CELL BI, 3(9), 2001, pp. 856-859

Abstract

Enteropathogenic Escherichia coli (EPEC) is a bacterial pathogen that causes infantile diarrhea worldwide(1). EPEC injects a bacterial protein, translocated intimin receptor (Tir), into the host-cell plasma membrane where itacts as a receptor for the bacterial outer membrane protein, intimin(2). The interaction of Tir and intimin triggers a marked rearrangement of the host actin cytoskeleton into pedestals beneath adherent bacteria. On deliveryinto host cells, EPEC Tir is phosphorylated on tyrosine 474 of the intracellular carboxy-terminal domain, an event that is required for pedestal formation(3). Despite its essential role, the function of Tir tyrosine phosphorylation has not yet been elucidated. Here we show that tyrosine 474 of Tir directly binds the host-cell adaptor protein Nck, and that Nck is required for the recruitment of both neural Wiskott-Aldrich-syndrome protein (N-WASP) and the actin-related protein (Arp)2/3 complex to the EPEC pedestal, directly linking Tir to the cytoskeleton. Cells with null alleles of both mammalian Nick genes are resistant to the effects of EPEC on the actin cytoskeleton. These results implicate Nick adaptors as host-cell determinants of EPEC virulence.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 13:09:57