RT info:eu-repo/semantics/article
T1 Characterization of new substrates targeted by yersinia tyrosine phosphatase YopH
A1 Puerta Turrillas, María Luisa de la
A1 Trinidad, Antonio G.
A1 Rodríguez, María del Carmen
A1 Bogetz, Jori
A1 Sánchez Crespo, Mariano
A1 Mustelin, Tomas
A1 Alonso, Andrés
A1 Bayón Prieto, Yolanda
K1 Bacterias
K1 Yersinia
K1 Tyrosine Phosphatase
K1 24 Ciencias de la Vida
AB YopH 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.
PB Public Library of Science
SN 1932-6203
YR 2009
FD 2009
LK https://uvadoc.uva.es/handle/10324/47496
UL https://uvadoc.uva.es/handle/10324/47496
LA eng
NO PLoS ONE, 2009, vol. 4, n. 2, p. e4431
NO Producción Científica
DS UVaDOC
RD 11-jul-2024