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Protein networks supporting AP-3 function in targeting lysosomal membrane proteins

MPG-Autoren
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Baust,  Thorsten
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Czupalla,  Cornelia
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Thiele,  Christoph
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Hoflack,  Bernard
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Zitation

Baust, T., Anitei, M., Czupalla, C., Parshyna, I., Bourel, L., Thiele, C., et al. (2008). Protein networks supporting AP-3 function in targeting lysosomal membrane proteins. Molecular Biology of the Cell, 19(5), 1942-1951.


Zitierlink: http://hdl.handle.net/21.11116/0000-0001-0E6E-6
Zusammenfassung
The AP-3 adaptor complex targets selected transmembrane proteins to lysosomes and lysosome-related organelles. We reconstituted its preferred interaction with liposomes containing the ADP ribosylation factor (ARF)-1 guanosine triphosphatase (GTPase), specific cargo tails, and phosphatidylinositol-3 phosphate, and then we performed a proteomic screen to identify new proteins supporting its sorting function. We identified approximately 30 proteins belonging to three networks regulating either AP-3 coat assembly or septin polymerization or Rab7-dependent lysosomal transport. RNA interference shows that, among these proteins, the ARF-1 exchange factor brefeldin A-inhibited exchange factor 1, the ARF-1 GTPase-activating protein 1, the Cdc42-interacting Cdc42 effector protein 4, an effector of septin-polymerizing GTPases, and the phosphatidylinositol-3 kinase IIIC3 are key components regulating the targeting of lysosomal membrane proteins to lysosomes in vivo. This analysis reveals that these proteins, together with AP-3, play an essential role in protein sorting at early endosomes, thereby regulating the integrity of these organelles.