Recruitment of arfaptins to the trans-Golgi network by PI(4)P and their involvement in cargo export
| Autor: | Julien Villeneuve, David Cruz-Garcia, Marko Jovic, Thomas Seufferlein, Tamas Balla, Marc Porzner, Margherita Scarpa, Vivek Malhotra, Maria Ortega-Bellido |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
Biological Transport
Active General Biochemistry Genetics and Molecular Biology Protein Structure Secondary Article 03 medical and health sciences symbols.namesake chemistry.chemical_compound 0302 clinical medicine Phosphatidylinositol Phosphates Chlorocebus aethiops BAR domain Animals Humans Phosphatidylinositol Phosphorylation Molecular Biology Protein kinase C Protein Kinase C 030304 developmental biology Adaptor Proteins Signal Transducing 0303 health sciences General Immunology and Microbiology biology General Neuroscience Chromogranin A Golgi apparatus Cell biology Protein Structure Tertiary Secretory protein Drosophila melanogaster HEK293 Cells chemistry Amphiphysin COS Cells Liposomes symbols biology.protein 030217 neurology & neurosurgery Biogenesis HeLa Cells trans-Golgi Network |
| Zdroj: | EMBO Journal. |
| Popis: | The BAR (Bin/Amphiphysin/Rvs) domain proteins arfaptin1 and arfaptin2 are localized to the trans-Golgi network (TGN) and, by virtue of their ability to sense and/or generate membrane curvature, could play an important role in the biogenesis of transport carriers. We report that arfaptins contain an amphipathic helix (AH) preceding the BAR domain, which is essential for their binding to phosphatidylinositol 4-phosphate (PI(4)P)-containing liposomes and the TGN of mammalian cells. The binding of arfaptin1, but not arfaptin2, to PI(4)P is regulated by protein kinase D (PKD) mediated phosphorylation at Ser100 within the AH. We also found that only arfaptin1 is required for the PKD-dependent trafficking of chromogranin A by the regulated secretory pathway. Altogether, these findings reveal the importance of PI(4)P and PKD in the recruitment of arfaptins at the TGN and their requirement in the events leading to the biogenesis of secretory storage granules. |
| Databáze: | OpenAIRE |
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