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http://purl.uniprot.org/citations/25049230http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25049230http://www.w3.org/2000/01/rdf-schema#comment"Homer proteins are scaffold molecules with a domain structure consisting of an N-terminal Ena/VASP homology 1 protein-binding domain and a C-terminal leucine zipper/coiled-coil domain. The Ena/VASP homology 1 domain recognizes proline-rich motifs and binds multiple Ca(2+)-signaling proteins, including G protein-coupled receptors, inositol 1,4,5-triphosphate receptors, ryanodine receptors, and transient receptor potential channels. However, their role in Ca(2+) signaling in nonexcitable cells is not well understood. In this study, we investigated the role of Homer2 on Ca(2+) signaling in parotid gland acinar cells using Homer2-deficient (Homer2(-/-)) mice. Homer2 is localized at the apical pole in acinar cells. Deletion of Homer2 did not affect inositol 1,4,5-triphosphate receptor localization or channel activity and did not affect the expression and activity of sarco/endoplasmic reticulum Ca(2+)-ATPase pumps. In contrast, Homer2 deletion markedly increased expression of plasma membrane Ca(2+)-ATPase (PMCA) pumps, in particular PMCA4, at the apical pole. Accordingly, Homer2 deficiency increased Ca(2+) extrusion by acinar cells. These findings were supported by co-immunoprecipitation of Homer2 and PMCA in wild-type parotid cells and transfected human embryonic kidney 293 (HEK293) cells. We identified a Homer-binding PPXXF-like motif in the N terminus of PMCA that is required for interaction with Homer2. Mutation of the PPXXF-like motif did not affect the interaction of PMCA with Homer1 but inhibited its interaction with Homer2 and increased Ca(2+) clearance by PMCA. These findings reveal an important regulation of PMCA by Homer2 that has a central role on PMCA-mediated Ca(2+) signaling in parotid acinar cells."xsd:string
http://purl.uniprot.org/citations/25049230http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m114.577221"xsd:string
http://purl.uniprot.org/citations/25049230http://purl.uniprot.org/core/author"Lee J."xsd:string
http://purl.uniprot.org/citations/25049230http://purl.uniprot.org/core/author"Park S."xsd:string
http://purl.uniprot.org/citations/25049230http://purl.uniprot.org/core/author"Jo H."xsd:string
http://purl.uniprot.org/citations/25049230http://purl.uniprot.org/core/author"Muallem S."xsd:string
http://purl.uniprot.org/citations/25049230http://purl.uniprot.org/core/author"Shin D.M."xsd:string
http://purl.uniprot.org/citations/25049230http://purl.uniprot.org/core/author"Yang Y.M."xsd:string
http://purl.uniprot.org/citations/25049230http://purl.uniprot.org/core/author"Chang I."xsd:string
http://purl.uniprot.org/citations/25049230http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/25049230http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/25049230http://purl.uniprot.org/core/pages"24971-24979"xsd:string
http://purl.uniprot.org/citations/25049230http://purl.uniprot.org/core/title"Homer2 protein regulates plasma membrane Ca^2⁺-ATPase-mediated Ca^2⁺ signaling in mouse parotid gland acinar cells."xsd:string
http://purl.uniprot.org/citations/25049230http://purl.uniprot.org/core/volume"289"xsd:string
http://purl.uniprot.org/citations/25049230http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/25049230
http://purl.uniprot.org/citations/25049230http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/25049230
http://purl.uniprot.org/uniprot/#_D1FNM8-mappedCitation-25049230http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25049230
http://purl.uniprot.org/uniprot/#_D1FNM9-mappedCitation-25049230http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25049230
http://purl.uniprot.org/uniprot/#_A0A140LHR9-mappedCitation-25049230http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25049230
http://purl.uniprot.org/uniprot/#_A0A140LJ06-mappedCitation-25049230http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25049230
http://purl.uniprot.org/uniprot/#_E9Q828-mappedCitation-25049230http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25049230
http://purl.uniprot.org/uniprot/#_F6V4K0-mappedCitation-25049230http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25049230
http://purl.uniprot.org/uniprot/#_H2BL43-mappedCitation-25049230http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25049230
http://purl.uniprot.org/uniprot/#_E9Q4F9-mappedCitation-25049230http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25049230