Sorting Nexin 17 Accelerates Internalization Yet Retards Degradation of P-selectin
| Autor: | Ross Williams, Thomas Schlüter, Peter Knauth, Marnie S. Roberts, Daniel F. Cutler, Ralf Bohnensack |
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| Rok vydání: | 2004 |
| Předmět: |
Endosome
Endocytic cycle Vesicular Transport Proteins Gene Expression Endosomes Biology Endocytosis Exocytosis Cell membrane Phosphatidylinositol 3-Kinases symbols.namesake medicine Animals Humans Sorting Nexins Molecular Biology Cells Cultured Phosphoinositide-3 Kinase Inhibitors Cell Membrane Articles Cell Biology Receptor-mediated endocytosis Golgi apparatus Protein Structure Tertiary Cell biology Androstadienes P-Selectin Protein Transport Sorting nexin medicine.anatomical_structure symbols Carrier Proteins Lysosomes Wortmannin |
| Zdroj: | Molecular Biology of the Cell. 15:3095-3105 |
| ISSN: | 1939-4586 1059-1524 |
| DOI: | 10.1091/mbc.e04-02-0143 |
| Popis: | The transient appearance of P-selectin on the surface of endothelial cells helps recruit leukocytes into sites of inflammation. The tight control of cell surface P-selectin on these cells depends on regulated exocytosis of Weibel-Palade bodies where the protein is stored and on its rapid endocytosis. After endocytosis, P-selectin is either sorted via endosomes and the Golgi apparatus for storage in Weibel-Palade bodies or targeted to lysosomes for degradation. A potential player in this complex endocytic itinerary is SNX17, a member of the sorting nexin family, which has been shown in a yeast two-hybrid assay to bind P-selectin. Here, we show that overexpression of SNX17 in mammalian cells can influence two key steps in the endocytic trafficking of P-selectin. First, it promotes the endocytosis of P-selectin from the plasma membrane. Second, it inhibits the movement of P-selectin into lysosomes, thereby reducing its degradation. |
| Databáze: | OpenAIRE |
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