Palmitoylation Targets CD39/Endothelial ATP Diphosphohydrolase to Caveolae
| Autor: | Olaf Guckelberger, Imrana Qawi, Christian Goepfert, Katarzyna Koziak, Elzbieta Kaczmarek, Masato Imai, Ágnes Kittel, Jan Krzysztof Blusztajn, Jean Sévigny, Jan Schulte am Esch, Simon C. Robson |
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| Rok vydání: | 2000 |
| Předmět: |
Cytoplasm
Glycosylation Blotting Western Palmitic Acid Biology Transfection Biochemistry chemistry.chemical_compound Palmitoylation Antigens CD Caveolae Extracellular Animals Humans Molecular Biology Integral membrane protein Cells Cultured Adenosine Triphosphatases Apyrase Cell Membrane Purinergic receptor Cell Biology Cell biology Microscopy Electron Transmembrane domain chemistry Mutagenesis COS Cells lipids (amino acids peptides and proteins) Chromatography Thin Layer Endothelium Vascular Lipid modification Signal Transduction |
| Zdroj: | Journal of Biological Chemistry. 275:2057-2062 |
| ISSN: | 0021-9258 |
| Popis: | Ectonucleotidases influence purinergic receptor function by the hydrolysis of extracellular nucleotides. CD39 is an integral membrane protein that is a prototype member of the nucleoside 5'-triphosphate diphosphohydrolase family. The native CD39 protein has two intracytoplasmic and two transmembrane domains. There is a large extracellular domain that undergoes extensive glycosylation and can be post-translationally modified by limited proteolysis. We have identified a potential thioester linkage site for S-acylation within the N-terminal region of CD39 and demonstrate that this region undergoes palmitoylation in a constitutive manner. The covalent lipid modification of this region of the protein appears to be important both in plasma membrane association and in targeting CD39 to caveolae. These specialized plasmalemmal domains are enriched in G protein-coupled receptors and appear to integrate cellular activation events. We suggest that palmitoylation could modulate the function of CD39 in regulating cellular signal transduction pathways. |
| Databáze: | OpenAIRE |
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