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Título

Characterization of new substrates targeted by Yersinia tyrosine phosphatase YopH

AutorPuerta, María Luisa de la; García Trinidad, Antonio ; Rodríguez, María del Carmen ; Bogetz, Jori; Sánchez Crespo, Mariano; Mustelin, Tomas; Alonso, Andrés ; Bayón, Yolanda
Fecha de publicación16-feb-2009
EditorPublic Library of Science
CitaciónPLoS ONE 4(2): e4431 (2009)
ResumenYopH is an exceptionally active tyrosine phosphatase that is essential for virulence of Yersinia pestis, the bacterium causing plague. YopH breaks down signal transduction mechanisms in immune cells and inhibits the immune response. Only a few substrates for YopH have been characterized so far, for instance p130Cas and Fyb, but in view of YopH potency and the great number of proteins involved in signalling pathways it is quite likely that more proteins are substrates of this phosphatase. In this respect, we show here YopH interaction with several proteins not shown before, such as Gab1, Gab2, p85, and Vav and analyse the domains of YopH involved in these interactions. Furthermore, we show that Gab1, Gab2 and Vav are not dephosphorylated by YopH, in contrast to Fyb, Lck, or p85, which are readily dephosphorylated by the phosphatase. These data suggests that YopH might exert its actions by interacting with adaptors involved in signal transduction pathways, what allows the phosphatase to reach and dephosphorylate its susbstrates.
Descripción8 páginas, 4 figuras.
Versión del editorhttp://dx.doi.org/10.1371/journal.pone.0004431
URIhttp://hdl.handle.net/10261/11874
DOI10.1371/journal.pone.0004431
ISSN1932-6203
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