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http://purl.uniprot.org/citations/14597204http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14597204http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14597204http://www.w3.org/2000/01/rdf-schema#comment"Spalten (Spn), a member of the PP2C family of Ser/Thr protein phosphatases, is required for Dictyostelium cell-type differentiation and morphogenesis. We have identified a new protein kinase, ARCK-1, through a second site suppressor screen for mutants that allow spn null cells to proceed further through development. ARCK-1 has a C-terminal kinase domain most closely related to Ser/Thr protein kinases and an N-terminal putative regulatory domain with ankyrin repeats, a 14-3-3 binding domain, and a C1 domain, which is required for binding to RasBGTP in a two-hybrid assay. Disruption of the gene encoding ARCK-1 results in weak, late developmental defects. However, overexpression of ARCK-1 phenocopies the spn null phenotype, consistent with Spn and ARCK-1 being on the same developmental pathway. Our previous analyses of Spn and the present analysis of ARCK-1 suggest a model in which Spn and ARCK-1 differentially control the phosphorylation state of a protein that regulates cell-type differentiation. Dephosphorylation of the substrate by Spn is required for cell-type differentiation. Control of ARCK-1 and Spn activities by upstream signals is proposed to be part of the developmental regulatory program mediating cell-fate decisions in Dictyostelium."xsd:string
http://purl.uniprot.org/citations/14597204http://purl.org/dc/terms/identifier"doi:10.1016/j.ydbio.2003.07.012"xsd:string
http://purl.uniprot.org/citations/14597204http://purl.org/dc/terms/identifier"doi:10.1016/j.ydbio.2003.07.012"xsd:string
http://purl.uniprot.org/citations/14597204http://purl.uniprot.org/core/author"Aubry L."xsd:string
http://purl.uniprot.org/citations/14597204http://purl.uniprot.org/core/author"Aubry L."xsd:string
http://purl.uniprot.org/citations/14597204http://purl.uniprot.org/core/author"Lee S."xsd:string
http://purl.uniprot.org/citations/14597204http://purl.uniprot.org/core/author"Lee S."xsd:string
http://purl.uniprot.org/citations/14597204http://purl.uniprot.org/core/author"Firtel R.A."xsd:string
http://purl.uniprot.org/citations/14597204http://purl.uniprot.org/core/author"Firtel R.A."xsd:string
http://purl.uniprot.org/citations/14597204http://purl.uniprot.org/core/author"Ravanel K."xsd:string
http://purl.uniprot.org/citations/14597204http://purl.uniprot.org/core/author"Ravanel K."xsd:string
http://purl.uniprot.org/citations/14597204http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/14597204http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/14597204http://purl.uniprot.org/core/name"Dev. Biol."xsd:string
http://purl.uniprot.org/citations/14597204http://purl.uniprot.org/core/name"Dev. Biol."xsd:string
http://purl.uniprot.org/citations/14597204http://purl.uniprot.org/core/pages"308-322"xsd:string
http://purl.uniprot.org/citations/14597204http://purl.uniprot.org/core/pages"308-322"xsd:string
http://purl.uniprot.org/citations/14597204http://purl.uniprot.org/core/title"The novel ankyrin-repeat containing kinase ARCK-1 acts as a suppressor of the Spalten signaling pathway during Dictyostelium development."xsd:string
http://purl.uniprot.org/citations/14597204http://purl.uniprot.org/core/title"The novel ankyrin-repeat containing kinase ARCK-1 acts as a suppressor of the Spalten signaling pathway during Dictyostelium development."xsd:string
http://purl.uniprot.org/citations/14597204http://purl.uniprot.org/core/volume"263"xsd:string
http://purl.uniprot.org/citations/14597204http://purl.uniprot.org/core/volume"263"xsd:string
http://purl.uniprot.org/citations/14597204http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14597204
http://purl.uniprot.org/citations/14597204http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14597204