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The glycolipid transfer protein interacts with the vesicle-associated membrane protein-associated protein VAP-A
- Source :
- Biochemical and Biophysical Research Communications. 388:395-399
- Publication Year :
- 2009
- Publisher :
- Elsevier BV, 2009.
-
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.
- Subjects :
- Synaptobrevin
Amino Acid Motifs
Molecular Sequence Data
Vesicular Transport Proteins
Biophysics
Biochemistry
Glycolipid
Humans
Amino Acid Sequence
Molecular Biology
Peptide sequence
Glutathione Transferase
chemistry.chemical_classification
biology
Endoplasmic reticulum
Cell Biology
Amino acid
Cell biology
Vesicle-associated membrane protein
chemistry
Glycolipid transfer protein
Mutation
biology.protein
Carrier Proteins
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 388
- Database :
- OpenAIRE
- Journal :
- Biochemical and Biophysical Research Communications
- Accession number :
- edsair.doi.dedup.....66f412f12a9cdd160ad937e30a2f75cc