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http://purl.uniprot.org/citations/12657671http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12657671http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12657671http://www.w3.org/2000/01/rdf-schema#comment"Proneuropeptides are packaged into dense-core vesicles in which they are processed into active peptides by copackaged enzymes. Proprotein convertases (PCs) cleave precursors after dibasic residues, and carboxypeptidases remove basic residues from the C terminals. We show here that the Caenorhabditis elegans egl-21 gene encodes a protein that is very similar to carboxypeptidase E (CPE) and is broadly expressed in the nervous system. Mutants lacking either egl-21 CPE or egl-3, which encodes the C. elegans ortholog of PC type 2 (PC2), were defective for processing endogenously expressed FMRFamide (Phe-Met-Arg-Phe-NH2)-related peptides (FaRPs). Mutants lacking the unc-104 kinesin motor protein were defective for anterograde movement of dense-core vesicle components, including egl-3 PC2, egl-21 CPE, and FaRPs. We provide evidence that egl-3 PC2 and egl-21 CPE mutants have diminished acetylcholine release at neuromuscular junctions (NMJs). Taken together, these results suggest that egl-21 CPE and egl-3 PC2 process endogenous neuropeptides that facilitate acetylcholine release at C. elegans NMJs."xsd:string
http://purl.uniprot.org/citations/12657671http://purl.org/dc/terms/identifier"doi:10.1523/jneurosci.23-06-02122.2003"xsd:string
http://purl.uniprot.org/citations/12657671http://purl.org/dc/terms/identifier"doi:10.1523/jneurosci.23-06-02122.2003"xsd:string
http://purl.uniprot.org/citations/12657671http://purl.uniprot.org/core/author"Kaplan J.M."xsd:string
http://purl.uniprot.org/citations/12657671http://purl.uniprot.org/core/author"Kaplan J.M."xsd:string
http://purl.uniprot.org/citations/12657671http://purl.uniprot.org/core/author"Jacob T.C."xsd:string
http://purl.uniprot.org/citations/12657671http://purl.uniprot.org/core/author"Jacob T.C."xsd:string
http://purl.uniprot.org/citations/12657671http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12657671http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12657671http://purl.uniprot.org/core/name"J. Neurosci."xsd:string
http://purl.uniprot.org/citations/12657671http://purl.uniprot.org/core/name"J. Neurosci."xsd:string
http://purl.uniprot.org/citations/12657671http://purl.uniprot.org/core/pages"2122-2130"xsd:string
http://purl.uniprot.org/citations/12657671http://purl.uniprot.org/core/pages"2122-2130"xsd:string
http://purl.uniprot.org/citations/12657671http://purl.uniprot.org/core/title"The EGL-21 carboxypeptidase E facilitates acetylcholine release at Caenorhabditis elegans neuromuscular junctions."xsd:string
http://purl.uniprot.org/citations/12657671http://purl.uniprot.org/core/title"The EGL-21 carboxypeptidase E facilitates acetylcholine release at Caenorhabditis elegans neuromuscular junctions."xsd:string
http://purl.uniprot.org/citations/12657671http://purl.uniprot.org/core/volume"23"xsd:string
http://purl.uniprot.org/citations/12657671http://purl.uniprot.org/core/volume"23"xsd:string
http://purl.uniprot.org/citations/12657671http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12657671
http://purl.uniprot.org/citations/12657671http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12657671
http://purl.uniprot.org/citations/12657671http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12657671
http://purl.uniprot.org/citations/12657671http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12657671
http://purl.uniprot.org/uniprot/P23678http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12657671
http://purl.uniprot.org/uniprot/G5ECN9http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12657671