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http://purl.uniprot.org/citations/17287461http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17287461http://www.w3.org/2000/01/rdf-schema#comment"A stable MIN6 beta-cell clone overexpressing glucokinase as an enhanced cyan fluorescent protein (ECFP) fusion construct was generated for analysis of glucokinase regulation in these glucose-responsive insulin-secreting cells. A higher glucokinase enzyme activity accompanied by an improved glucose-induced insulin secretion indicated the integration of ECFP-glucokinase into the functional pool of glucokinase protein in MIN6-ECFP-glucokinase cells. Fluorescence recovery after photobleaching experiments of MIN6-ECFP-glucokinase cells and photoactivation of a transiently transfected photoswitchable cyan fluorescent protein (PS-CFP)-glucokinase construct in MIN6 cells indicate a higher motility of the diffusible glucokinase fraction at high glucose concentrations. In agreement with previous studies, we observed significant binding of ECFP-glucokinase to insulin secretory granules. Using fluorescence lifetime imaging, we obtained evidence for an association between glucokinase and alpha-tubulin in MIN6-ECFP-glucokinase cells. Furthermore, immunohistochemistry and fluorescence resonance energy transfer analysis by acceptor photobleaching showed distinct association between endogenous glucokinase and alpha-tubulin as well as beta-tubulin in MIN6 cells. Interestingly, glucokinase was also colocalized with kinesin, a motor protein involved in insulin secretory granule movement. Therefore, we suggest a role of a bound glucokinase protein fraction in the regulation of insulin granule movement along tubulin filaments."xsd:string
http://purl.uniprot.org/citations/17287461http://purl.org/dc/terms/identifier"doi:10.2337/db06-0894"xsd:string
http://purl.uniprot.org/citations/17287461http://purl.uniprot.org/core/author"Baltrusch S."xsd:string
http://purl.uniprot.org/citations/17287461http://purl.uniprot.org/core/author"Lenzen S."xsd:string
http://purl.uniprot.org/citations/17287461http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17287461http://purl.uniprot.org/core/name"Diabetes"xsd:string
http://purl.uniprot.org/citations/17287461http://purl.uniprot.org/core/pages"1305-1315"xsd:string
http://purl.uniprot.org/citations/17287461http://purl.uniprot.org/core/title"Novel insights into the regulation of the bound and diffusible glucokinase in MIN6 beta-cells."xsd:string
http://purl.uniprot.org/citations/17287461http://purl.uniprot.org/core/volume"56"xsd:string
http://purl.uniprot.org/citations/17287461http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17287461
http://purl.uniprot.org/citations/17287461http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17287461
http://purl.uniprot.org/uniprot/#_P52792-mappedCitation-17287461http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17287461
http://purl.uniprot.org/uniprot/#_Q5SVI5-mappedCitation-17287461http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17287461
http://purl.uniprot.org/uniprot/#_Q5SVI6-mappedCitation-17287461http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17287461
http://purl.uniprot.org/uniprot/#_Q6LE83-mappedCitation-17287461http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17287461
http://purl.uniprot.org/uniprot/Q5SVI6http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17287461
http://purl.uniprot.org/uniprot/P52792http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17287461
http://purl.uniprot.org/uniprot/Q5SVI5http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17287461
http://purl.uniprot.org/uniprot/Q6LE83http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17287461