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http://purl.uniprot.org/citations/15317815http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15317815http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15317815http://www.w3.org/2000/01/rdf-schema#comment"The acid-sensing ion channel-3 (ASIC3) is a degenerin/epithelial sodium channel expressed in the peripheral nervous system. Previous studies indicate that it participates in the response to mechanical and painful stimuli, perhaps contributing to mechanoreceptor and/or H+ -gated nociceptor function. ASIC3 subunits contain intracellular N and C termini that may control channel localization and function. We found that a PDZ-binding motif at the ASIC3 C terminus interacts with four different proteins that contain PDZ domains: PSD-95, Lin-7b, MAGI-1b, and PIST. ASIC3 and these interacting proteins were expressed in dorsal root ganglia and spinal cord, and PSD-95 co-precipitated ASIC3 from spinal cord. When expressed in heterologous cells, PSD-95 reduced the amplitude of ASIC3 acid-evoked currents, whereas Lin-7b increased current amplitude. PSD-95 and Lin-7b altered current density by decreasing or increasing, respectively, the amount of ASIC3 on the cell surface. The finding that multiple PDZ-containing proteins bind ASIC3 and can influence its presence in the plasma membrane suggests that they may play an important role in the contribution of ASIC3 to nociception and mechanosensation."xsd:string
http://purl.uniprot.org/citations/15317815http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m405874200"xsd:string
http://purl.uniprot.org/citations/15317815http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m405874200"xsd:string
http://purl.uniprot.org/citations/15317815http://purl.uniprot.org/core/author"Welsh M.J."xsd:string
http://purl.uniprot.org/citations/15317815http://purl.uniprot.org/core/author"Welsh M.J."xsd:string
http://purl.uniprot.org/citations/15317815http://purl.uniprot.org/core/author"Benson C.J."xsd:string
http://purl.uniprot.org/citations/15317815http://purl.uniprot.org/core/author"Benson C.J."xsd:string
http://purl.uniprot.org/citations/15317815http://purl.uniprot.org/core/author"Hruska-Hageman A.M."xsd:string
http://purl.uniprot.org/citations/15317815http://purl.uniprot.org/core/author"Hruska-Hageman A.M."xsd:string
http://purl.uniprot.org/citations/15317815http://purl.uniprot.org/core/author"Leonard A.S."xsd:string
http://purl.uniprot.org/citations/15317815http://purl.uniprot.org/core/author"Leonard A.S."xsd:string
http://purl.uniprot.org/citations/15317815http://purl.uniprot.org/core/author"Price M.P."xsd:string
http://purl.uniprot.org/citations/15317815http://purl.uniprot.org/core/author"Price M.P."xsd:string
http://purl.uniprot.org/citations/15317815http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15317815http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15317815http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15317815http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15317815http://purl.uniprot.org/core/pages"46962-46968"xsd:string
http://purl.uniprot.org/citations/15317815http://purl.uniprot.org/core/pages"46962-46968"xsd:string
http://purl.uniprot.org/citations/15317815http://purl.uniprot.org/core/title"PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current."xsd:string
http://purl.uniprot.org/citations/15317815http://purl.uniprot.org/core/title"PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current."xsd:string
http://purl.uniprot.org/citations/15317815http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/15317815http://purl.uniprot.org/core/volume"279"xsd:string