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

被引:27
作者
Tuuf, Jessica [1 ]
Wistbacka, Lina [1 ]
Mattjus, Peter [1 ]
机构
[1] Abo Akad Univ, Dept Biochem & Pharm, FI-20520 Turku, Finland
基金
芬兰科学院;
关键词
Glycolipid transfer protein; GLTP; Vesicle-associated membrane protein-associated proteins; VAP-A; FFAT; Glycosphingolipids; Synaptobrevin; Endoplasmic reticulum; Lipid transfer; OXYSTEROL-BINDING PROTEIN; FFAT MOTIF; ENDOPLASMIC-RETICULUM; STRUCTURAL BASIS; VAMP; CERAMIDE; IDENTIFICATION; TRAFFICKING;
D O I
10.1016/j.bbrc.2009.08.023
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 2009 Elsevier Inc. All rights reserved.
引用
收藏
页码:395 / 399
页数:5
相关论文
共 20 条
[1]   DETERMINATION OF THE INTRACELLULAR SITES AND TOPOLOGY OF GLUCOSYLCERAMIDE SYNTHESIS IN RAT-LIVER [J].
FUTERMAN, AH ;
PAGANO, RE .
BIOCHEMICAL JOURNAL, 1991, 280 :295-302
[2]   Molecular machinery for non-vesicular trafficking of ceramide [J].
Hanada, K ;
Kumagai, K ;
Yasuda, S ;
Miura, Y ;
Kawano, M ;
Fukasawa, M ;
Nishijima, M .
NATURE, 2003, 426 (6968) :803-809
[3]   Structural basis of FFAT motif-mediated ER targeting [J].
Kaiser, SE ;
Brickner, JH ;
Reilein, AR ;
Fenn, TD ;
Walter, P ;
Brunger, AT .
STRUCTURE, 2005, 13 (07) :1035-1045
[4]   Efficient trafficking of ceramide from the endoplasmic reticulum to the Golgi apparatus requires a VAMP-associated protein-interacting FFAT motif of CERT [J].
Kawano, Miyuki ;
Kumagai, Keigo ;
Nishijima, Masahiro ;
Hanada, Kentaro .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (40) :30279-30288
[5]   A highly conserved binding site in vesicle-associated membrane protein-associated protein (VAP) for the FFAT motif of lipid-binding proteins [J].
Loewen, CJR ;
Levine, TP .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (14) :14097-14104
[6]   A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP [J].
Loewen, CJR ;
Roy, A ;
Levine, TP .
EMBO JOURNAL, 2003, 22 (09) :2025-2035
[7]  
LOWRY OH, 1951, J BIOL CHEM, V193, P265
[8]   Structural basis for glycosphingolipid transfer specificity [J].
Malinina, L ;
Malakhova, ML ;
Teplov, A ;
Brown, RE ;
Patel, DJ .
NATURE, 2004, 430 (7003) :1048-1053
[9]   Charged membrane surfaces impede the protein-mediated transfer of glycosphingolipids between phospholipid bilayers [J].
Mattjus, P ;
Pike, HM ;
Molotkovsky, JG ;
Brown, RE .
BIOCHEMISTRY, 2000, 39 (05) :1067-1075
[10]   Glycolipid transfer proteins and membrane interaction [J].
Mattjus, Peter .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2009, 1788 (01) :267-272