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http://purl.uniprot.org/citations/29180010http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/29180010http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/29180010http://www.w3.org/2000/01/rdf-schema#comment"Cardiolipin and phosphatidic acid-binding protein (CLPABP) controls the stability of the mRNA harboring an AU-rich element (ARE) in the 3' UTR with the help of the RNA stabilizer, human antigen R (HuR). Although CLPABP is localized on the mitochondrial surface as a large protein-RNA complex, its precise role is not yet known. Recently, CLPABP was identified as an N-myristoylated protein. Here, we demonstrate the effects of N-myristoylation on the functions of CLPABP. In the present study, compared to the wild-type protein that possessed the "MG" motif at the N-terminus for N-myristoylation, the mutant CLPABP protein that lacked N-myristoylation modification site was unstable. Furthermore, the expression of the G/A mutant of CLPABP, which lacked N-myristoylation site, induced morphological alterations in mitochondria. Because pleckstrin homology domain-deleted mutant, which was fused with the N-myristoylation site derived from intact CLPABP, could not colocalize with mitochondria, N-myristoylation of CLPABP was predicted to affect its stability onto the mitochondrial membrane rather than its subcellular localization."xsd:string
http://purl.uniprot.org/citations/29180010http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2017.11.112"xsd:string
http://purl.uniprot.org/citations/29180010http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2017.11.112"xsd:string
http://purl.uniprot.org/citations/29180010http://purl.uniprot.org/core/author"Maeda A."xsd:string
http://purl.uniprot.org/citations/29180010http://purl.uniprot.org/core/author"Maeda A."xsd:string
http://purl.uniprot.org/citations/29180010http://purl.uniprot.org/core/author"Nishino T."xsd:string
http://purl.uniprot.org/citations/29180010http://purl.uniprot.org/core/author"Nishino T."xsd:string
http://purl.uniprot.org/citations/29180010http://purl.uniprot.org/core/author"Nishikawa S."xsd:string
http://purl.uniprot.org/citations/29180010http://purl.uniprot.org/core/author"Nishikawa S."xsd:string
http://purl.uniprot.org/citations/29180010http://purl.uniprot.org/core/author"Uchida M."xsd:string
http://purl.uniprot.org/citations/29180010http://purl.uniprot.org/core/author"Uchida M."xsd:string
http://purl.uniprot.org/citations/29180010http://purl.uniprot.org/core/author"Konishi H."xsd:string
http://purl.uniprot.org/citations/29180010http://purl.uniprot.org/core/author"Konishi H."xsd:string
http://purl.uniprot.org/citations/29180010http://purl.uniprot.org/core/date"2018"xsd:gYear
http://purl.uniprot.org/citations/29180010http://purl.uniprot.org/core/date"2018"xsd:gYear
http://purl.uniprot.org/citations/29180010http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/29180010http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/29180010http://purl.uniprot.org/core/pages"1249-1256"xsd:string
http://purl.uniprot.org/citations/29180010http://purl.uniprot.org/core/pages"1249-1256"xsd:string
http://purl.uniprot.org/citations/29180010http://purl.uniprot.org/core/title"Role of N-myristoylation in stability and subcellular localization of the CLPABP protein."xsd:string
http://purl.uniprot.org/citations/29180010http://purl.uniprot.org/core/title"Role of N-myristoylation in stability and subcellular localization of the CLPABP protein."xsd:string
http://purl.uniprot.org/citations/29180010http://purl.uniprot.org/core/volume"495"xsd:string
http://purl.uniprot.org/citations/29180010http://purl.uniprot.org/core/volume"495"xsd:string