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http://purl.uniprot.org/citations/27979965http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27979965http://www.w3.org/2000/01/rdf-schema#comment"The intracellular signaling protein regulator of presynaptic morphology 1 (RPM-1) is a conserved regulator of synapse formation and axon termination in Caenorhabditis elegans RPM-1 functions in a ubiquitin ligase complex with the F-box protein FSN-1 and functions through the microtubule binding protein RAE-1. Using a structure-function approach and positive selection for transgenic C. elegans, we explored the biochemical relationship between RPM-1, FSN-1, and RAE-1. This led to the identification of two new domains in RPM-1 that are sufficient for binding to FSN-1, called FSN-1 binding domain 2 (FBD2) and FBD3. Furthermore, we map the RAE-1 binding domain to a much smaller region of RPM-1. Point mutations in RPM-1 that reduce binding to RAE-1 did not affect FSN-1 binding, indicating that RPM-1 utilizes different biochemical mechanisms to bind these molecules. Analysis of RPM-1 protein complexes in the neurons of C. elegans elucidated two further discoveries: FSN-1 binds to RAE-1, and this interaction is not mediated by RPM-1, and RPM-1 binding to FSN-1 and RAE-1 reduces FSN-1·RAE-1 complex formation. These results indicate that RPM-1 uses different mechanisms to recruit FSN-1 and RAE-1 into independent signaling complexes in neurons."xsd:string
http://purl.uniprot.org/citations/27979965http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m116.748004"xsd:string
http://purl.uniprot.org/citations/27979965http://purl.uniprot.org/core/author"Grill B."xsd:string
http://purl.uniprot.org/citations/27979965http://purl.uniprot.org/core/author"Baker S.T."xsd:string
http://purl.uniprot.org/citations/27979965http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/27979965http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/27979965http://purl.uniprot.org/core/pages"2519-2530"xsd:string
http://purl.uniprot.org/citations/27979965http://purl.uniprot.org/core/title"Defining Minimal Binding Regions in Regulator of Presynaptic Morphology 1 (RPM-1) Using Caenorhabditis elegans Neurons Reveals Differential Signaling Complexes."xsd:string
http://purl.uniprot.org/citations/27979965http://purl.uniprot.org/core/volume"292"xsd:string
http://purl.uniprot.org/citations/27979965http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/27979965
http://purl.uniprot.org/citations/27979965http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/27979965
http://purl.uniprot.org/uniprot/#_Q17551-mappedCitation-27979965http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27979965
http://purl.uniprot.org/uniprot/#_Q18223-mappedCitation-27979965http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27979965
http://purl.uniprot.org/uniprot/#_Q93454-mappedCitation-27979965http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27979965
http://purl.uniprot.org/uniprot/Q93454http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/27979965
http://purl.uniprot.org/uniprot/Q17551http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/27979965
http://purl.uniprot.org/uniprot/Q18223http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/27979965