Biochimica et Biophysica Acta (BBA) - Biomembranes
Volume 1798, Issue 11, November 2010, Pages 2094-2101
The multidrug resistance half-transporter ABCG2 is purified as a tetramer upon selective extraction from membranes☆
Under an Elsevier user license
open archive
Research Highlights
►His-ABCG2 was purified onto functionalised lipid surfaces ►Electron microscopy and biochemical analysis revealed tetramers of ABCG2 ►Tetramers of ABCG2 were purified after expression in Sf9 insect or in human cells
Abbreviations
ABC
ATP-binding cassette
BSA
bovine serum albumin, CHAPS, 3-[(3-cholamidopropyl) dimethylammonio]-1-propanesulfonate
cmc
critical micelle concentration
DDM
dodecyl-β-D-maltoside
DOTM
dodecyl-β-D-thiomaltoside
DOPC
dioleyl-phospatidyl choline
DMPC
dimiristoyl-phosphatidylcholine
EM
electron microscopy
Fos-choline 16
n-Hexadecylphosphocholine
MDR
multidrug resistance
NBD
nucleotide-binding domain
NEM
N-ethylmaleimide
Ni-NTA DOGS
Ni-nitrilotriacetic-1,2-dioleoyl-sn-glycero-3-{[N (5-Amino-1-Carboxypentyl) iminodiacetic Acid]Succinyl
TM
transmembrane domain
Keywords
Multidrug resistance
ABCG2
Functionalized lipid layer
Electron microscopy
Sf9 insect cells
Flp-In-293 cells
Cited by (0)
- ☆
This work was supported by the Institut Curie, CNRS and Université Lyon 1 (UMR 5086) and grants from the Agence Nationale de la Recherche (ANR-06-BLAN-0420, ANR-PCV06-135269 and ANR-PCV06-135175), and the Ligue Nationale contre le Cancer (ADP & PF, Equipe Labellisée Ligue 2009).
Copyright © 2010 Elsevier B.V. All rights reserved.