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

A1 Journal article (refereed)


Internal Authors/Editors


Publication Details

List of Authors: Tuuf J, Wistbacka L, Mattjus P
Publication year: 2009
Journal: Biochemical and Biophysical Research Communications
Volume number: 388
Issue number: 2
Start page: 395
End page: 399
ISSN: 0006-291X
eISSN: 1090-2104


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.

Last updated on 2019-19-10 at 02:43