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http://purl.uniprot.org/citations/9450989http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9450989http://www.w3.org/2000/01/rdf-schema#comment"The uptake step of receptor-mediated endocytosis in yeast is dependent on the calcium binding protein calmodulin (Cmd1p). In order to understand the role that Cmd1p plays, a search was carried out for possible targets among the genes required for the internalization process. Co-immunoprecipitation, two-hybrid and overlay assays demonstrated that Cmd1p interacts with Myo5p, a type I unconventional myosin. Analysis of the endocytic phenotype and the Cmd1p-Myo5p interaction in thermosensitive cmd1 mutants indicated that the Cmd1p-Myo5p interaction is required for endocytosis in vivo. However, the Cmd1p-Myo5p interaction requirement was partially overcome by deleting the calmodulin binding sites (IQ motifs) from Myo5p, suggesting that these motifs inhibit Myo5p function. Additionally, genetic and biochemical evidence obtained with a collection of cmd1 mutant alleles strongly suggests that Cmd1p plays an additional role in the internalization step of receptor-mediated endocytosis in yeast."xsd:string
http://purl.uniprot.org/citations/9450989http://purl.org/dc/terms/identifier"doi:10.1093/emboj/17.3.635"xsd:string
http://purl.uniprot.org/citations/9450989http://purl.uniprot.org/core/author"Riezman H."xsd:string
http://purl.uniprot.org/citations/9450989http://purl.uniprot.org/core/author"Geli M.I."xsd:string
http://purl.uniprot.org/citations/9450989http://purl.uniprot.org/core/author"Wesp A."xsd:string
http://purl.uniprot.org/citations/9450989http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9450989http://purl.uniprot.org/core/name"EMBO J"xsd:string
http://purl.uniprot.org/citations/9450989http://purl.uniprot.org/core/pages"635-647"xsd:string
http://purl.uniprot.org/citations/9450989http://purl.uniprot.org/core/title"Distinct functions of calmodulin are required for the uptake step of receptor-mediated endocytosis in yeast: the type I myosin Myo5p is one of the calmodulin targets."xsd:string
http://purl.uniprot.org/citations/9450989http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/9450989http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9450989
http://purl.uniprot.org/citations/9450989http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9450989
http://purl.uniprot.org/uniprot/P06787#attribution-62E29148201F0031785DB992EBBCC6EFhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/9450989
http://purl.uniprot.org/uniprot/#_P06787-mappedCitation-9450989http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9450989
http://purl.uniprot.org/uniprot/#_Q04439-mappedCitation-9450989http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9450989
http://purl.uniprot.org/uniprot/P06787http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/9450989
http://purl.uniprot.org/uniprot/Q04439http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/9450989