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http://purl.uniprot.org/citations/12514244http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12514244http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12514244http://www.w3.org/2000/01/rdf-schema#comment"Protein phosphorylation has pivotal roles in ABA and osmotic stress signaling in higher plants. Two protein phosphatase genes, ABI1 and ABI2, are known to regulate these signaling pathways in Arabidopsis: The identity of ABA-activated protein kinases required for the ABA signaling, however, remains to be elucidated. Here we demonstrate that two protein kinases, p44 and p42, were activated by ABA in Arabidopsis T87 cultured cells, and at least one protein kinase, p44, was activated not only by ABA but also by low humidity in Arabidopsis plants. Analysis of T-DNA knockout mutants and biochemical analysis using a specific antibody revealed that the p44 is encoded by a SnRK2-type protein kinase gene, SRK2E. The srk2e mutation resulted in a wilty phenotype mainly due to loss of stomatal closure in response to a rapid humidity decrease. ABA-inducible gene expression of rd22 and rd29B was suppressed in srk2e. These results show that SRK2E plays an important role in ABA signaling in response to water stress."xsd:string
http://purl.uniprot.org/citations/12514244http://purl.org/dc/terms/identifier"doi:10.1093/pcp/pcf188"xsd:string
http://purl.uniprot.org/citations/12514244http://purl.org/dc/terms/identifier"doi:10.1093/pcp/pcf188"xsd:string
http://purl.uniprot.org/citations/12514244http://purl.uniprot.org/core/author"Ecker J.R."xsd:string
http://purl.uniprot.org/citations/12514244http://purl.uniprot.org/core/author"Ecker J.R."xsd:string
http://purl.uniprot.org/citations/12514244http://purl.uniprot.org/core/author"Shinozaki K."xsd:string
http://purl.uniprot.org/citations/12514244http://purl.uniprot.org/core/author"Shinozaki K."xsd:string
http://purl.uniprot.org/citations/12514244http://purl.uniprot.org/core/author"Takahashi F."xsd:string
http://purl.uniprot.org/citations/12514244http://purl.uniprot.org/core/author"Takahashi F."xsd:string
http://purl.uniprot.org/citations/12514244http://purl.uniprot.org/core/author"Mizoguchi T."xsd:string
http://purl.uniprot.org/citations/12514244http://purl.uniprot.org/core/author"Mizoguchi T."xsd:string
http://purl.uniprot.org/citations/12514244http://purl.uniprot.org/core/author"Ichimura K."xsd:string
http://purl.uniprot.org/citations/12514244http://purl.uniprot.org/core/author"Ichimura K."xsd:string
http://purl.uniprot.org/citations/12514244http://purl.uniprot.org/core/author"Yoshida R."xsd:string
http://purl.uniprot.org/citations/12514244http://purl.uniprot.org/core/author"Yoshida R."xsd:string
http://purl.uniprot.org/citations/12514244http://purl.uniprot.org/core/author"Hobo T."xsd:string
http://purl.uniprot.org/citations/12514244http://purl.uniprot.org/core/author"Hobo T."xsd:string
http://purl.uniprot.org/citations/12514244http://purl.uniprot.org/core/author"Aronso J."xsd:string
http://purl.uniprot.org/citations/12514244http://purl.uniprot.org/core/author"Aronso J."xsd:string
http://purl.uniprot.org/citations/12514244http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12514244http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12514244http://purl.uniprot.org/core/name"Plant Cell Physiol."xsd:string
http://purl.uniprot.org/citations/12514244http://purl.uniprot.org/core/name"Plant Cell Physiol."xsd:string