The glycolipid transfer protein interacts with the vesicle-associated membrane protein-associated protein VAP-A

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    Abstract

    The glycolipid transfer protein (GLTP) is a cytoplasmic protein with an ability to bind glycolipids and catalyze their in vitro transfer. In this study, we have found a FFAT-like motif in GLTP. The FFAT (two phenylalanines in an acidic tract) motif in lipid-binding proteins has previously been shown to interact with the VAPs (vesicle-associated membrane protein-associated proteins) in the endoplasmic reticulum. Here we used glutathione S-transferase pull-down experiments to confirm that GLTP and VAP-A interact. By displacing different amino acids in the motif we clearly show that the interaction is dependent on the FFAT-like motif in GLTP. The potential role of GLTP in the endoplasmic reticulum association is discussed.
    Original languageUndefined/Unknown
    Pages (from-to)395–399
    JournalBiochemical and Biophysical Research Communications
    Volume388
    Issue number2
    DOIs
    Publication statusPublished - 2009
    MoE publication typeA1 Journal article-refereed

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