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 language | Undefined/Unknown |
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Pages (from-to) | 395–399 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 388 |
Issue number | 2 |
DOIs | |
Publication status | Published - 2009 |
MoE publication type | A1 Journal article-refereed |