Role of N-myristoylation in stability and subcellular localization of the CLPABP protein
| Autor: | Akane Maeda, Moe Uchida, Hiroaki Konishi, Tasuku Nishino, Sumire Nishikawa |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Untranslated region Biophysics Protein Prenylation Biochemistry Myristic Acid 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Chlorocebus aethiops Cardiolipin Animals Humans Inner mitochondrial membrane Molecular Biology Lipid-Linked Proteins Messenger RNA Cell Biology Subcellular localization Lipid Metabolism Protein subcellular localization prediction Cell biology Pleckstrin homology domain 030104 developmental biology HEK293 Cells chemistry COS Cells Protein prenylation lipids (amino acids peptides and proteins) 030217 neurology & neurosurgery Subcellular Fractions |
| Zdroj: | Biochemical and biophysical research communications. 495(1) |
| ISSN: | 1090-2104 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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