Characterization of new substrates targeted by Yersinia tyrosine phosphatase YopH.

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...

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Autores principales:	María Luisa de la Puerta, Antonio G Trinidad, María del Carmen Rodríguez, Jori Bogetz, Mariano Sánchez Crespo, Tomas Mustelin, Andrés Alonso, Yolanda Bayón
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2009
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/84489e9b27a14c8eadd827df4021d2b3
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spelling	oai:doaj.org-article:84489e9b27a14c8eadd827df4021d2b32021-11-25T06:17:17ZCharacterization of new substrates targeted by Yersinia tyrosine phosphatase YopH.1932-620310.1371/journal.pone.0004431https://doaj.org/article/84489e9b27a14c8eadd827df4021d2b32009-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19221593/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203YopH 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.María Luisa de la PuertaAntonio G TrinidadMaría del Carmen RodríguezJori BogetzMariano Sánchez CrespoTomas MustelinAndrés AlonsoYolanda BayónPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 4, Iss 2, p e4431 (2009)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q María Luisa de la Puerta Antonio G Trinidad María del Carmen Rodríguez Jori Bogetz Mariano Sánchez Crespo Tomas Mustelin Andrés Alonso Yolanda Bayón Characterization of new substrates targeted by Yersinia tyrosine phosphatase YopH.
description	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.
format	article
author	María Luisa de la Puerta Antonio G Trinidad María del Carmen Rodríguez Jori Bogetz Mariano Sánchez Crespo Tomas Mustelin Andrés Alonso Yolanda Bayón
author_facet	María Luisa de la Puerta Antonio G Trinidad María del Carmen Rodríguez Jori Bogetz Mariano Sánchez Crespo Tomas Mustelin Andrés Alonso Yolanda Bayón
author_sort	María Luisa de la Puerta
title	Characterization of new substrates targeted by Yersinia tyrosine phosphatase YopH.
title_short	Characterization of new substrates targeted by Yersinia tyrosine phosphatase YopH.
title_full	Characterization of new substrates targeted by Yersinia tyrosine phosphatase YopH.
title_fullStr	Characterization of new substrates targeted by Yersinia tyrosine phosphatase YopH.
title_full_unstemmed	Characterization of new substrates targeted by Yersinia tyrosine phosphatase YopH.
title_sort	characterization of new substrates targeted by yersinia tyrosine phosphatase yoph.
publisher	Public Library of Science (PLoS)
publishDate	2009
url	https://doaj.org/article/84489e9b27a14c8eadd827df4021d2b3
work_keys_str_mv	AT marialuisadelapuerta characterizationofnewsubstratestargetedbyyersiniatyrosinephosphataseyoph AT antoniogtrinidad characterizationofnewsubstratestargetedbyyersiniatyrosinephosphataseyoph AT mariadelcarmenrodriguez characterizationofnewsubstratestargetedbyyersiniatyrosinephosphataseyoph AT joribogetz characterizationofnewsubstratestargetedbyyersiniatyrosinephosphataseyoph AT marianosanchezcrespo characterizationofnewsubstratestargetedbyyersiniatyrosinephosphataseyoph AT tomasmustelin characterizationofnewsubstratestargetedbyyersiniatyrosinephosphataseyoph AT andresalonso characterizationofnewsubstratestargetedbyyersiniatyrosinephosphataseyoph AT yolandabayon characterizationofnewsubstratestargetedbyyersiniatyrosinephosphataseyoph
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Characterization of new substrates targeted by Yersinia tyrosine phosphatase YopH.

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