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http://purl.uniprot.org/citations/10590166http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10590166http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10590166http://www.w3.org/2000/01/rdf-schema#comment"Members of the Arabidopsis calcineurin B-like Ca(2)+ binding protein (AtCBL) family are differentially regulated by stress conditions. One AtCBL plays a role in salt stress; another is implicated in response to other stress signals, including drought, cold, and wounding. In this study, we identified a group of novel protein kinases specifically associated with AtCBL-type Ca(2)+ sensors. In addition to a typical protein kinase domain, they all contain a unique C-terminal region that is both required and sufficient for interaction with the AtCBL-type but not calmodulin-type Ca(2)+ binding proteins from plants. Interactions between the kinases and AtCBLs require micromolar concentrations of Ca(2)+, suggesting that increases in cellular Ca(2)+ concentrations may trigger the formation of AtCBL-kinase complexes in vivo. Unlike most serine/threonine kinases, the AtCBL-interacting kinase efficiently uses Mn(2)+ to Mg(2)+ as a cofactor and may function as a Mn(2)+ binding protein in the cell. These findings link a new type of Ca(2)+ sensors to a group of novel protein kinases, providing the molecular basis for a unique Ca(2)+ signaling machinery in plant cells."xsd:string
http://purl.uniprot.org/citations/10590166http://purl.org/dc/terms/identifier"doi:10.1105/tpc.11.12.2393"xsd:string
http://purl.uniprot.org/citations/10590166http://purl.org/dc/terms/identifier"doi:10.1105/tpc.11.12.2393"xsd:string
http://purl.uniprot.org/citations/10590166http://purl.uniprot.org/core/author"Gupta R."xsd:string
http://purl.uniprot.org/citations/10590166http://purl.uniprot.org/core/author"Gupta R."xsd:string
http://purl.uniprot.org/citations/10590166http://purl.uniprot.org/core/author"Shi J."xsd:string
http://purl.uniprot.org/citations/10590166http://purl.uniprot.org/core/author"Shi J."xsd:string
http://purl.uniprot.org/citations/10590166http://purl.uniprot.org/core/author"Albrecht V."xsd:string
http://purl.uniprot.org/citations/10590166http://purl.uniprot.org/core/author"Albrecht V."xsd:string
http://purl.uniprot.org/citations/10590166http://purl.uniprot.org/core/author"Luan S."xsd:string
http://purl.uniprot.org/citations/10590166http://purl.uniprot.org/core/author"Luan S."xsd:string
http://purl.uniprot.org/citations/10590166http://purl.uniprot.org/core/author"Harter K."xsd:string
http://purl.uniprot.org/citations/10590166http://purl.uniprot.org/core/author"Harter K."xsd:string
http://purl.uniprot.org/citations/10590166http://purl.uniprot.org/core/author"Kudla J."xsd:string
http://purl.uniprot.org/citations/10590166http://purl.uniprot.org/core/author"Kudla J."xsd:string
http://purl.uniprot.org/citations/10590166http://purl.uniprot.org/core/author"Kim K.-N."xsd:string
http://purl.uniprot.org/citations/10590166http://purl.uniprot.org/core/author"Kim K.-N."xsd:string
http://purl.uniprot.org/citations/10590166http://purl.uniprot.org/core/author"Ritz O."xsd:string
http://purl.uniprot.org/citations/10590166http://purl.uniprot.org/core/author"Ritz O."xsd:string
http://purl.uniprot.org/citations/10590166http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10590166http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10590166http://purl.uniprot.org/core/name"Plant Cell"xsd:string
http://purl.uniprot.org/citations/10590166http://purl.uniprot.org/core/name"Plant Cell"xsd:string