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http://purl.uniprot.org/citations/18390926http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18390926http://www.w3.org/2000/01/rdf-schema#comment"Phospholipase Cbeta1 (PLCbeta1) exists as two splice variants, PLCbeta1a (150 kDa) and PLCbeta1b (140 kDa), which differ only in their C-terminal sequences of 64 and 31 amino acids, respectively. The 3 C-terminal amino acid residues of PLCbeta1a comprise a PDZ-interacting domain, whereas the PLCbeta1b sequence has no PDZ-interacting domain but contains unique proline-rich domain 5 residues from the C terminus. PLCbeta1a is localized in the cytoplasm, whereas PLCbeta1b targets to the sarcolemma and is enriched in caveolae. Deletion of 3 amino acids from the C terminus of PLCbeta1b did not alter its sarcolemmal localization, but deletion of the entire unique 31 amino acid sequence caused cytosolic localization. A myristoylated 10 amino acid peptide from the C terminus of PLCbeta1b selectively dissociated N-terminally GFP-tagged PLCbeta1b from the sarcolemma and inhibited PLC responses to alpha(1)-adrenergic agonists, with a half maximal effective concentration of 12 +/-1.6 microM (mean+/-SE, n=3). A similar peptide from PLCbeta1a was without effect at concentrations below 100 microM. Thus, the extreme C-terminal sequences of the PLCbeta1 splice variants determine localization and, thus, function. In cardiomyocytes, responses initiated by alpha(1)-adrenergic receptor activation involve only PLCbeta1b, and the selective targeting of this splice variant to the sarcolemma provides a potential therapeutic target to reduce hypertrophy, apoptosis, and arrhythmias."xsd:string
http://purl.uniprot.org/citations/18390926http://purl.org/dc/terms/identifier"doi:10.1096/fj.07-102558"xsd:string
http://purl.uniprot.org/citations/18390926http://purl.uniprot.org/core/author"Huynh H."xsd:string
http://purl.uniprot.org/citations/18390926http://purl.uniprot.org/core/author"Woodcock E.A."xsd:string
http://purl.uniprot.org/citations/18390926http://purl.uniprot.org/core/author"Vasilevski O."xsd:string
http://purl.uniprot.org/citations/18390926http://purl.uniprot.org/core/author"Grubb D.R."xsd:string
http://purl.uniprot.org/citations/18390926http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18390926http://purl.uniprot.org/core/name"FASEB J"xsd:string
http://purl.uniprot.org/citations/18390926http://purl.uniprot.org/core/pages"2768-2774"xsd:string
http://purl.uniprot.org/citations/18390926http://purl.uniprot.org/core/title"The extreme C-terminal region of phospholipase Cbeta1 determines subcellular localization and function; the "b" splice variant mediates alpha1-adrenergic receptor responses in cardiomyocytes."xsd:string
http://purl.uniprot.org/citations/18390926http://purl.uniprot.org/core/volume"22"xsd:string
http://purl.uniprot.org/citations/18390926http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18390926
http://purl.uniprot.org/citations/18390926http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18390926
http://purl.uniprot.org/uniprot/#_A6HQI6-mappedCitation-18390926http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18390926
http://purl.uniprot.org/uniprot/#_P10687-mappedCitation-18390926http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18390926
http://purl.uniprot.org/uniprot/#_R9PXY3-mappedCitation-18390926http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18390926
http://purl.uniprot.org/uniprot/A6HQI6http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18390926
http://purl.uniprot.org/uniprot/R9PXY3http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18390926
http://purl.uniprot.org/uniprot/P10687http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18390926