期刊
MOLECULAR BIOLOGY OF THE CELL
卷 19, 期 5, 页码 1942-1951出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E08-02-0110
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- TU-Dresden [HWP-1207]
- SMWK-EFRE [1203]
- Bundesministerium fur Bildung und Forschung [0313815B]
- Deutsche Forschungsgemeinschaft [TRR 13/2-08, HO 2584/2-1, HO 2584/1-1]
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 approximate to 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.
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