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...
| Main Authors: | , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2009-01-01
|
| Series: | PLoS ONE |
| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19221593/pdf/?tool=EBI |
| _version_ | 1818984014803894272 |
|---|---|
| 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 |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-20T18:12:16Z |
| format | Article |
| id | doaj.art-84489e9b27a14c8eadd827df4021d2b3 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-20T18:12:16Z |
| publishDate | 2009-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-84489e9b27a14c8eadd827df4021d2b32022-12-21T19:30:27ZengPublic Library of Science (PLoS)PLoS ONE1932-62032009-01-0142e443110.1371/journal.pone.0004431Characterization of new substrates targeted by Yersinia tyrosine phosphatase YopH.María Luisa de la PuertaAntonio G TrinidadMaría del Carmen RodríguezJori BogetzMariano Sánchez CrespoTomas MustelinAndrés AlonsoYolanda BayónYopH 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.https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19221593/pdf/?tool=EBI |
| spellingShingle | 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. PLoS ONE |
| title | 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_short | Characterization of new substrates targeted by Yersinia tyrosine phosphatase YopH. |
| title_sort | characterization of new substrates targeted by yersinia tyrosine phosphatase yoph |
| url | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19221593/pdf/?tool=EBI |
| 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 |