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FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P

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Anna Godi, Antonella Di Campli, Athanasios Konstantakopoulos, Giuseppe Di Tullio, Dario R Alessi, Gursant S Kular, Tiziana Daniele, Pierfrancesco Marra, John M Lucocq, M Antonietta De Matteis

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The molecular mechanisms underlying the formation of carriers trafficking from the Golgi complex to the cell surface are still ill-defined; nevertheless, the involvement of a lipid-based machinery is well established. This includes phosphatidylinositol 4-phosphate (PtdIns(4)P), the precursor for phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P(2)). In yeast, PtdIns(4)P exerts a direct role, however, its mechanism of action and its targets in mammalian cells remain uncharacterized. We have identified two effectors of PtdIns(4)P, the four-phosphate-adaptor protein 1 and 2 (FAPP1 and FAPP2). Both proteins localize to the trans-Golgi network (TGN) on nascent carriers, and interact with PtdIns(4)P and the small GTPase ADP-ribosylation factor (ARF) through their plekstrin homology (PH) domain. Displacement or knockdown of FAPPs inhibits cargo transfer to the plasma membrane. Moreover, overexpression of FAPP-PH impairs carrier fission. Therefore, FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery that controls generation of constitutive post-Golgi carriers.


Original languageEnglish
Pages (from-to)393-404
Number of pages12
JournalNature Cell Biology
Issue number5
Publication statusPublished - May 2004

    Research areas

  • ADP-Ribosylation Factors, Adaptor Proteins, Signal Transducing, Animals, Biological Transport, COS Cells, Carrier Proteins, Cell Membrane, Fungal Proteins, Golgi Apparatus, Humans, Molecular Sequence Data, Phosphatidylinositol Phosphates, Protein Structure, Tertiary, RNA, Small Interfering, Recombinant Fusion Proteins, Subcellular Fractions, trans-Golgi Network

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