Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide

@article{DAngelo2007GlycosphingolipidSR,
  title={Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide},
  author={Giovanni D’Angelo and Elena Polishchuk and Giuseppe Di Tullio and Michele Santoro and Antonella di Campli and Anna Godi and Gun West and Jacek Bielawski and Chia-Chen Chuang and Aarnoud C. van der Spoel and Frances M. Platt and Yusuf A. Hannun and Roman S. Polishchuk and Peter Mattjus and Maria Antonietta De Matteis},
  journal={Nature},
  year={2007},
  volume={449},
  pages={62-67}
}
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… 
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TLDR
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TLDR
The crystal structure of the GLTP homology (GLTPH) domain of human 4-phosphate adaptor protein 2 (FAPP2) bound with N-oleoyl-galactosylceramide is reported, revealing an element, termed the ID loop, that controls specificity in theGLTP family.
Metabolic pathways and intracellular trafficking of gangliosides
TLDR
A number of enzymes for ganglioside anabolism and catabolism have been shown to be associated with the plasma membrane, which might contribute to modulate local glycolipid composition, and consequently, the cell function.
Sphingolipid transfer proteins defined by the GLTP-fold
TLDR
Glycolipid transfer proteins originally were identified as small, soluble, amphitropic proteins that specifically accelerate the intermembrane transfer of glycolipids but now are known to adopt a unique, helically dominated, two-layer ‘sandwich’ architecture defined as the GLTP-fold that provides the structural underpinning for the eukaryotic GLTP superfamily.
Specificity of the mammalian glycolipid transfer proteins.
  • P. Mattjus
  • Chemistry, Medicine
    Chemistry and physics of lipids
  • 2016
TLDR
This review summarizes what is structurally required by the glycosphingolipids in order for them to be transported by the GLTPs.
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