Sammanfattning
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.
Originalspråk | Odefinierat/okänt |
---|---|
Sidor (från-till) | 395–399 |
Tidskrift | Biochemical and Biophysical Research Communications |
Volym | 388 |
Nummer | 2 |
DOI | |
Status | Publicerad - 2009 |
MoE-publikationstyp | A1 Tidskriftsartikel-refererad |