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http://purl.uniprot.org/citations/12480930http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12480930http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12480930http://www.w3.org/2000/01/rdf-schema#comment"Regulation of Ca(2+) transporters is a vital component of signaling. The Arabidopsis H(+)/Ca(2+) exchanger CAX1 contains an N-terminal autoinhibitory domain that prevents Ca(2+) transport when CAX1 is heterologously expressed in yeast. Using a yeast screen, we have identified three different proteins that activate CAX1. One of these, CXIP1 (CAX-interacting protein-1; 19.3 kDa) has amino acid similarity to the C terminus of PICOT (protein kinase C-interacting cousin of thioredoxin) proteins. Although PICOT proteins are found in a variety of organisms, a function has not been previously ascribed to a plant PICOT protein. We demonstrate that CXIP1 activated the CAX1 homolog CAX4, but not CAX2 or CAX3. An Arabidopsis homolog of CXIP1 (CXIP2) weakly activated CAX4, but not CAX1. In a yeast two-hybrid assay, CXIP1 interacted with the N terminus of CAX1. In competition analysis, CXIP1 and a CAX1 N-terminal peptide appeared to bind to similar N-terminal domains of CAX1. Chimeric CAX3 constructs containing the N terminus of CAX1 were activated by CXIP1. In Arabidopsis, CXIP1 transcripts, like CAX1, accumulated in response to different metal conditions. This work thus characterizes a new class of signaling molecules in plants that may regulate CAX transporters in vivo."xsd:string
http://purl.uniprot.org/citations/12480930http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m210883200"xsd:string
http://purl.uniprot.org/citations/12480930http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m210883200"xsd:string
http://purl.uniprot.org/citations/12480930http://purl.uniprot.org/core/author"Cheng N.-H."xsd:string
http://purl.uniprot.org/citations/12480930http://purl.uniprot.org/core/author"Cheng N.-H."xsd:string
http://purl.uniprot.org/citations/12480930http://purl.uniprot.org/core/author"Hirschi K.D."xsd:string
http://purl.uniprot.org/citations/12480930http://purl.uniprot.org/core/author"Hirschi K.D."xsd:string
http://purl.uniprot.org/citations/12480930http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12480930http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12480930http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12480930http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12480930http://purl.uniprot.org/core/pages"6503-6509"xsd:string
http://purl.uniprot.org/citations/12480930http://purl.uniprot.org/core/pages"6503-6509"xsd:string
http://purl.uniprot.org/citations/12480930http://purl.uniprot.org/core/title"Cloning and characterization of CXIP1 A novel PICOT domain-containing Arabidopsis protein that associates with CAX1."xsd:string
http://purl.uniprot.org/citations/12480930http://purl.uniprot.org/core/title"Cloning and characterization of CXIP1 A novel PICOT domain-containing Arabidopsis protein that associates with CAX1."xsd:string
http://purl.uniprot.org/citations/12480930http://purl.uniprot.org/core/volume"278"xsd:string
http://purl.uniprot.org/citations/12480930http://purl.uniprot.org/core/volume"278"xsd:string
http://purl.uniprot.org/citations/12480930http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12480930
http://purl.uniprot.org/citations/12480930http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12480930
http://purl.uniprot.org/citations/12480930http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12480930
http://purl.uniprot.org/citations/12480930http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12480930
http://purl.uniprot.org/uniprot/Q8H7F6http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12480930
http://purl.uniprot.org/uniprot/Q39253http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12480930