Transition from dimers to higher oligomeric forms occurs during the ATPase cycle of the ABCA1 transporter.
Fluorescence resonance energy transfer and native PAGE analytical techniques were employed to assess the quaternary structure of ABCA1, an ATP binding cassette transporter playing a crucial role in cellular lipid handling. These experimental approaches support the conclusion that ABCA1 is associated in dimeric structures that undergo transition into higher order structures, i.e. tetramers, during the ATP catalytic cycle. Our data hence underline molecular assembly as a crucial parameter in ABCA1 function and the advantage of native PAGE as analytical tool for intractable membrane proteins.
Trompier
Doriane
D
Centre d'Immunologie de Marseille-Luminy, INSERM, CNRS, UniversitédelaMéditerranée, Parc Scientifique de Luminy, 13288 Marseille Cedex 09, France.
Alibert
Mélanie
M
Davanture
Suzel
S
Hamon
Yannick
Y
Pierres
Michel
M
Chimini
Giovanna
G
D064286:ATP Binding Cassette Transporter 1; D018528:ATP-Binding Cassette Transporters / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002384:Catalysis; D019281:Dimerization; D004591:Electrophoresis, Polyacrylamide Gel; D031541:Fluorescence Resonance Energy Transfer; D006367:HeLa Cells; D006801:Humans; D007700:Kinetics; D046911:Macromolecular Substances; D010957:Plasmids; D020836:Protein Structure, Quaternary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
C577836:ABCA1 protein, human; D064286:ATP Binding Cassette Transporter 1; D018528:ATP-Binding Cassette Transporters; D046911:Macromolecular Substances; D011994:Recombinant Proteins; D000251:Adenosine Triphosphatases