| http://purl.uniprot.org/citations/19107198 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19107198 | http://www.w3.org/2000/01/rdf-schema#comment | "PTPN3 and PTPN4 are two closely-related non-receptor protein tyrosine phosphatases (PTP) that, in addition to a PTP domain, contain FERM (Band 4.1, Ezrin, Radixin, and Moesin) and PDZ (PSD-95, Dlg, ZO-1) domains. Both PTP have been implicated as negative-regulators of early signal transduction through the T cell antigen receptor (TCR), acting to dephosphorylate the TCRzeta chain, a component of the TCR complex. Previously, we reported upon the production and characterization of PTPN3-deficient mice which show normal TCR signal transduction and T cell function. To address if the lack of a T cell phenotype in PTPN3-deficient mice can be explained by functional redundancy of PTPN3 with PTPN4, we generated PTPN4-deficient and PTPN4/PTPN3 double-deficient mice. As in PTPN3 mutants, T cell development and homeostasis and TCR-induced cytokine synthesis and proliferation were found to be normal in PTPN4-deficient and PTPN4/PTPN3 double-deficient mice. PTPN13 is another FERM and PDZ domain-containing non-receptor PTP that is distantly-related to PTPN3 and PTPN4 and which has been shown to function as a negative-regulator of T helper-1 (Th1) and Th2 differentiation. Therefore, to determine if PTPN13 might compensate for the loss of PTPN3 and PTPN4 in T cells, we generated mice that lack functional forms of all three PTP. T cells from triple-mutant mice developed normally and showed normal cytokine secretion and proliferative responses to TCR stimulation. Furthermore, T cell differentiation along the Th1, Th2 and Th17 lineages was largely unaffected in triple-mutants. We conclude that PTPN3 and PTPN4 are dispensable for TCR signal transduction."xsd:string |
| http://purl.uniprot.org/citations/19107198 | http://purl.org/dc/terms/identifier | "doi:10.1371/journal.pone.0004014"xsd:string |
| http://purl.uniprot.org/citations/19107198 | http://purl.uniprot.org/core/author | "King P.D."xsd:string |
| http://purl.uniprot.org/citations/19107198 | http://purl.uniprot.org/core/author | "Hendriks W.J."xsd:string |
| http://purl.uniprot.org/citations/19107198 | http://purl.uniprot.org/core/author | "Bauler T.J."xsd:string |
| http://purl.uniprot.org/citations/19107198 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/19107198 | http://purl.uniprot.org/core/name | "PLoS One"xsd:string |
| http://purl.uniprot.org/citations/19107198 | http://purl.uniprot.org/core/pages | "e4014"xsd:string |
| http://purl.uniprot.org/citations/19107198 | http://purl.uniprot.org/core/title | "The FERM and PDZ domain-containing protein tyrosine phosphatases, PTPN4 and PTPN3, are both dispensable for T cell receptor signal transduction."xsd:string |
| http://purl.uniprot.org/citations/19107198 | http://purl.uniprot.org/core/volume | "3"xsd:string |
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