The BAR domain protein Arfaptin-1 controls secretory granule biogenesis at the trans-golgi network
Summary BAR domains can prevent membrane fission through their ability to shield necks of budding vesicles from fission-inducing factors. However, the physiological role of this inhibitory function and its regulation is unknown. Here we identify a checkpoint involving the BAR-domain-containing prote...
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| Hauptverfasser: | , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
13 September 2012
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| In: |
Developmental cell
Year: 2012, Jahrgang: 23, Heft: 4, Pages: 756-768 |
| ISSN: | 1878-1551 |
| DOI: | 10.1016/j.devcel.2012.07.019 |
| Online-Zugang: | Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1016/j.devcel.2012.07.019 Verlag, kostenfrei, Volltext: http://www.sciencedirect.com/science/article/pii/S1534580712003383 
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| Verfasserangaben: | Helmuth Gehart, Alexander Goginashvili, Rainer Beck, Joëlle Morvan, Eric Erbs, Ivan Formentini, Maria Antonietta De Matteis, Yannick Schwab, Felix T. Wieland and Romeo Ricci |
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| 245 | 1 | 4 | |a The BAR domain protein Arfaptin-1 controls secretory granule biogenesis at the trans-golgi network |c Helmuth Gehart, Alexander Goginashvili, Rainer Beck, Joëlle Morvan, Eric Erbs, Ivan Formentini, Maria Antonietta De Matteis, Yannick Schwab, Felix T. Wieland and Romeo Ricci |
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| 520 | |a Summary BAR domains can prevent membrane fission through their ability to shield necks of budding vesicles from fission-inducing factors. However, the physiological role of this inhibitory function and its regulation is unknown. Here we identify a checkpoint involving the BAR-domain-containing protein Arfaptin-1 that controls biogenesis of secretory granules at the trans-Golgi network (TGN). We demonstrate that protein kinase D (PKD) phosphorylates Arfaptin-1 at serine 132, which disrupts the ability of Arfaptin-1 to inhibit the activity of ADP ribosylation factor, an important component of the vesicle scission machinery. The physiological significance of this regulatory mechanism is evidenced by loss of glucose-stimulated insulin secretion due to granule scission defects in pancreatic β cells expressing nonphosphorylatable Arfaptin-1. Accordingly, depletion of Arfaptin-1 leads to the generation of small nonfunctional secretory granules. Hence, PKD-mediated Arfaptin-1 phosphorylation is necessary to ensure biogenesis of functional transport carriers at the TGN in regulated secretion. | ||
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