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MBC in Press, published online ahead of print February 20, 2008
Mol. Biol. Cell 10.1091/mbc.E08-02-0110

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Submitted on February 1, 2008
Revised on February 7, 2008
Accepted on February 12, 2008

Protein Networks Supporting AP-3 Function in Targeting Lysosomal Membrane Proteins

Mihaela Anitei,*{dagger} Thorsten Baust,*{dagger} Cornelia Czupalla,*{dagger} Iryna Parshyna,* Line Bourel,{ddagger} Christoph Thiele,{sect} Eberhard Krause,|| and Bernard Hoflack*

*Biotechnological Center, Dresden University of Technology, 01307 Dresden, Germany; {ddagger}Faculté de Pharmacie de Lille, Laboratoire de Chimie, BP 83 59006 Lille Cedex, France; {sect}Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany; ||Institute of Molecular Pharmacology, 10 13125, Berlin, Germany

Monitoring Editor: Sandra Schmid

The AP-3 adaptor complex targets selected transmembrane proteins to lysosomes and lysosome-related organelles. We reconstituted its preferred interaction with liposomes containing the ARF-1 GTPase, specific cargo tails and phosphatidylinositol-3 phosphate and then performed a proteomic screen to identify new proteins supporting its sorting function. We identified {approx}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 Big1, the ARF-1 GTPase activating protein ARAP1, the Cdc42-interacting Borg4, 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.

{dagger}These authors contributed equally to this work.

Address correspondence to: Bernard Hoflack (bernard.hoflack{at}biotec.tu-dresden.de)




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