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http://purl.uniprot.org/citations/8491190http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8491190http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8491190http://www.w3.org/2000/01/rdf-schema#comment"Two novel protein kinase C (PKC)-like genes, pck1+ and pck2+ were isolated from fission yeast by PCR. Both contain common domains of PKC-related molecules, but lack a putative Ca(2+)-binding domain so that they may belong to the nPKC group. Gene disruption of pck1+ and pck2+ establishes that they share an overlapping essential function for cell viability. Cells of a single pck2 deletion display severe defects in cell shape; they are irregular and sometimes pear-like instead of cylindrical. In contrast, the induced overexpression of pck2+ is lethal, producing multiseptated and branched cells. These results suggest that fission yeast PKC-like genes are involved in the polarity of cell growth control. We show that pck2 is allelic to sts6, a locus we have previously identified by its supersensitivity to staurosporine, a potent protein kinase inhibitor [Toda et al. (1991) Genes Dev., 5, 60-73]. In addition, the lethal overexpression of pck2+ can be suppressed by staurosporine, indicating that fission yeast pck1 and pck2 are molecular targets of this inhibitor."xsd:string
http://purl.uniprot.org/citations/8491190http://purl.org/dc/terms/identifier"doi:10.1002/j.1460-2075.1993.tb05848.x"xsd:string
http://purl.uniprot.org/citations/8491190http://purl.org/dc/terms/identifier"doi:10.1002/j.1460-2075.1993.tb05848.x"xsd:string
http://purl.uniprot.org/citations/8491190http://purl.uniprot.org/core/author"Yanagida M."xsd:string
http://purl.uniprot.org/citations/8491190http://purl.uniprot.org/core/author"Yanagida M."xsd:string
http://purl.uniprot.org/citations/8491190http://purl.uniprot.org/core/author"Shimanuki M."xsd:string
http://purl.uniprot.org/citations/8491190http://purl.uniprot.org/core/author"Shimanuki M."xsd:string
http://purl.uniprot.org/citations/8491190http://purl.uniprot.org/core/author"Toda T."xsd:string
http://purl.uniprot.org/citations/8491190http://purl.uniprot.org/core/author"Toda T."xsd:string
http://purl.uniprot.org/citations/8491190http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8491190http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8491190http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/8491190http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/8491190http://purl.uniprot.org/core/pages"1987-1995"xsd:string
http://purl.uniprot.org/citations/8491190http://purl.uniprot.org/core/pages"1987-1995"xsd:string
http://purl.uniprot.org/citations/8491190http://purl.uniprot.org/core/title"Two novel protein kinase C-related genes of fission yeast are essential for cell viability and implicated in cell shape control."xsd:string
http://purl.uniprot.org/citations/8491190http://purl.uniprot.org/core/title"Two novel protein kinase C-related genes of fission yeast are essential for cell viability and implicated in cell shape control."xsd:string
http://purl.uniprot.org/citations/8491190http://purl.uniprot.org/core/volume"12"xsd:string
http://purl.uniprot.org/citations/8491190http://purl.uniprot.org/core/volume"12"xsd:string
http://purl.uniprot.org/citations/8491190http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8491190
http://purl.uniprot.org/citations/8491190http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8491190
http://purl.uniprot.org/citations/8491190http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8491190
http://purl.uniprot.org/citations/8491190http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8491190