The glycolipid transfer protein interacts with the vesicle-associated membrane protein-associated protein VAP-A.
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.
Tuuf
Jessica
J
Department of Biochemistry and Pharmacy, Abo Akademi University, FI-20520 Turku, Finland.
Wistbacka
Lina
L
Mattjus
Peter
P
D020816:Amino Acid Motifs / Q000235:genetics; D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D005982:Glutathione Transferase / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D009154:Mutation; D033921:Vesicular Transport Proteins / Q000235:genetics / Q000378:metabolism*
D002352:Carrier Proteins; C511922:GLTP protein, human; C114051:VAPA protein, human; D033921:Vesicular Transport Proteins; D005982:Glutathione Transferase