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http://purl.uniprot.org/citations/26644582http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26644582http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26644582http://www.w3.org/2000/01/rdf-schema#comment"Protein palmitoylation regulates many aspects of cell function and is carried out by acyl transferases that contain zf-DHHC motifs. The in vivo physiological function of protein palmitoylation is largely unknown. Here we generated mice deficient in the acyl transferase Aph2 (Ablphilin 2 or zf-DHHC16) and demonstrated an essential role for Aph2 in embryonic/postnatal survival, eye development, and heart development. Aph2(-/-) embryos and pups showed cardiomyopathy and cardiac defects including bradycardia. We identified phospholamban, a protein often associated with human cardiomyopathy, as an interacting partner and a substrate of Aph2. Aph2-mediated palmitoylation of phospholamban on cysteine 36 differentially alters its interaction with PKA and protein phosphatase 1 α, augmenting serine 16 phosphorylation, and regulates phospholamban pentamer formation. Aph2 deficiency results in phospholamban hypophosphorylation, a hyperinhibitory form. Ablation of phospholamban in Aph2(-/-) mice histologically and functionally alleviated the heart defects. These findings establish Aph2 as a critical in vivo regulator of cardiac function and reveal roles for protein palmitoylation in the development of other organs including eyes."xsd:string
http://purl.uniprot.org/citations/26644582http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1518368112"xsd:string
http://purl.uniprot.org/citations/26644582http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1518368112"xsd:string
http://purl.uniprot.org/citations/26644582http://purl.uniprot.org/core/author"Chen Y.H."xsd:string
http://purl.uniprot.org/citations/26644582http://purl.uniprot.org/core/author"Chen Y.H."xsd:string
http://purl.uniprot.org/citations/26644582http://purl.uniprot.org/core/author"Liu H."xsd:string
http://purl.uniprot.org/citations/26644582http://purl.uniprot.org/core/author"Liu H."xsd:string
http://purl.uniprot.org/citations/26644582http://purl.uniprot.org/core/author"Li J."xsd:string
http://purl.uniprot.org/citations/26644582http://purl.uniprot.org/core/author"Li J."xsd:string
http://purl.uniprot.org/citations/26644582http://purl.uniprot.org/core/author"Li B."xsd:string
http://purl.uniprot.org/citations/26644582http://purl.uniprot.org/core/author"Li B."xsd:string
http://purl.uniprot.org/citations/26644582http://purl.uniprot.org/core/author"Jia H."xsd:string
http://purl.uniprot.org/citations/26644582http://purl.uniprot.org/core/author"Jia H."xsd:string
http://purl.uniprot.org/citations/26644582http://purl.uniprot.org/core/author"Zhao P."xsd:string
http://purl.uniprot.org/citations/26644582http://purl.uniprot.org/core/author"Zhao P."xsd:string
http://purl.uniprot.org/citations/26644582http://purl.uniprot.org/core/author"He L."xsd:string
http://purl.uniprot.org/citations/26644582http://purl.uniprot.org/core/author"He L."xsd:string
http://purl.uniprot.org/citations/26644582http://purl.uniprot.org/core/author"Goff S.P."xsd:string
http://purl.uniprot.org/citations/26644582http://purl.uniprot.org/core/author"Goff S.P."xsd:string
http://purl.uniprot.org/citations/26644582http://purl.uniprot.org/core/author"Zhou T."xsd:string
http://purl.uniprot.org/citations/26644582http://purl.uniprot.org/core/author"Zhou T."xsd:string
http://purl.uniprot.org/citations/26644582http://purl.uniprot.org/core/author"Boast S."xsd:string
http://purl.uniprot.org/citations/26644582http://purl.uniprot.org/core/author"Boast S."xsd:string