Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide

Giovanni D’Angelo, Elena Polishchuk, Giuseppe Di Tullio, Michele Santoro, Antonella Di Campli, Anna Godi, Gun West, Jacek Bielawski, Chia-Chen Chuang, Aarnoud C. van der Spoel, Frances M. Platt, Yusuf A. Hannun, Roman Polishchuk, Peter Mattjus and Maria Antonietta De Matteis ()
Additional contact information
Giovanni D’Angelo: Consorzio Mario Negri Sud, Via Nazionale 8/A, 66030 Santa Maria Imbaro, Chieti, Italy
Elena Polishchuk: Consorzio Mario Negri Sud, Via Nazionale 8/A, 66030 Santa Maria Imbaro, Chieti, Italy
Giuseppe Di Tullio: Consorzio Mario Negri Sud, Via Nazionale 8/A, 66030 Santa Maria Imbaro, Chieti, Italy
Michele Santoro: Consorzio Mario Negri Sud, Via Nazionale 8/A, 66030 Santa Maria Imbaro, Chieti, Italy
Antonella Di Campli: Consorzio Mario Negri Sud, Via Nazionale 8/A, 66030 Santa Maria Imbaro, Chieti, Italy
Anna Godi: Consorzio Mario Negri Sud, Via Nazionale 8/A, 66030 Santa Maria Imbaro, Chieti, Italy
Gun West: Åbo Akademi University, Artillerigatan 6 A III, BioCity FI-20520 Turku, Finland
Jacek Bielawski: Medical University of South Carolina, 173 Ashley Avenue, Charleston, South Carolina 29425, USA
Chia-Chen Chuang: University of Oxford, Mansfield Road, Oxford OX1 3QT, UK
Aarnoud C. van der Spoel: University of Oxford, Mansfield Road, Oxford OX1 3QT, UK
Frances M. Platt: University of Oxford, Mansfield Road, Oxford OX1 3QT, UK
Yusuf A. Hannun: Medical University of South Carolina, 173 Ashley Avenue, Charleston, South Carolina 29425, USA
Roman Polishchuk: Consorzio Mario Negri Sud, Via Nazionale 8/A, 66030 Santa Maria Imbaro, Chieti, Italy
Peter Mattjus: Åbo Akademi University, Artillerigatan 6 A III, BioCity FI-20520 Turku, Finland
Maria Antonietta De Matteis: Consorzio Mario Negri Sud, Via Nazionale 8/A, 66030 Santa Maria Imbaro, Chieti, Italy

Nature, 2007, vol. 449, issue 7158, 62-67

Abstract: Abstract The molecular machinery responsible for the generation of transport carriers moving from the Golgi complex to the plasma membrane relies on a tight interplay between proteins and lipids. Among the lipid-binding proteins of this machinery, we previously identified the four-phosphate adaptor protein FAPP2, the pleckstrin homology domain of which binds phosphatidylinositol 4-phosphate and the small GTPase ARF1. FAPP2 also possesses a glycolipid-transfer-protein homology domain. Here we show that human FAPP2 is a glucosylceramide-transfer protein that has a pivotal role in the synthesis of complex glycosphingolipids, key structural and signalling components of the plasma membrane. The requirement for FAPP2 makes the whole glycosphingolipid synthetic pathway sensitive to regulation by phosphatidylinositol 4-phosphate and ARF1. Thus, by coupling the synthesis of glycosphingolipids with their export to the cell surface, FAPP2 emerges as crucial in determining the lipid identity and composition of the plasma membrane.

Date: 2007
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DOI: 10.1038/nature06097

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