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.
journal_name
Naturejournal_title
Natureauthors
D'Angelo G,Polishchuk E,Di Tullio G,Santoro M,Di Campli A,Godi A,West G,Bielawski J,Chuang CC,van der Spoel AC,Platt FM,Hannun YA,Polishchuk R,Mattjus P,De Matteis MAdoi
10.1038/nature06097subject
Has Abstractpub_date
2007-09-06 00:00:00pages
62-7issue
7158eissn
0028-0836issn
1476-4687pii
nature06097journal_volume
449pub_type
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