Characterization of New Substrates Targeted By Yersinia Tyrosine Phosphatase YopH
Open Access
- 16 February 2009
- journal article
- research article
- Published by Public Library of Science (PLoS) in PLOS ONE
- Vol. 4 (2), e4431
- https://doi.org/10.1371/journal.pone.0004431
Abstract
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.This publication has 36 references indexed in Scilit:
- The multiple function of Grb2 associated binder (Gab) adaptor/scaffolding protein in immune cell signalingImmunology Letters, 2006
- YERSINIA OUTER PROTEINS: Role in Modulation of Host Cell Signaling Responses and PathogenesisAnnual Review of Microbiology, 2005
- The adaptor molecules LAT and SLP-76 are specifically targeted by Yersinia to inhibit T cell activationThe Journal of Experimental Medicine, 2005
- Two substrate‐targeting sites in the Yersinia protein tyrosine phosphatase co‐operate to promote bacterial virulenceMolecular Microbiology, 2005
- YopH prevents monocyte chemoattractant protein 1 expression in macrophages and T‐cell proliferation through inactivation of the phosphatidylinositoI 3‐kinase pathwayMolecular Microbiology, 2002
- Vav proteins, adaptors and cell signalingOncogene, 2001
- Identification of Residues in the N-terminal Domain of theYersinia Tyrosine Phosphatase That Are Critical for Substrate RecognitionPublished by Elsevier BV ,2001
- The Yersinia Yop virulon: a bacterial system for subverting eukaryotic cellsMolecular Microbiology, 1997
- Relationship Between Virulence and Immunity as Revealed in Recent Studies of the Fl Capsule of Yersinia pestisClinical Infectious Diseases, 1995
- Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 Å and the complex with tungstateNature, 1994