Transition from Dimers to Higher Oligomeric Forms Occurs during the ATPase Cycle of the ABCA1 Transporter
Copyright policy )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.
Adenosine Triphosphatases, [SDV.IMM] Life Sciences [q-bio]/Immunology, Macromolecular Substances, Catalysis, Recombinant Proteins, Kinetics, Fluorescence Resonance Energy Transfer, Humans, ATP-Binding Cassette Transporters, Electrophoresis, Polyacrylamide Gel, Protein Structure, Quaternary, Dimerization, ATP Binding Cassette Transporter 1, HeLa Cells, Plasmids
Adenosine Triphosphatases, [SDV.IMM] Life Sciences [q-bio]/Immunology, Macromolecular Substances, Catalysis, Recombinant Proteins, Kinetics, Fluorescence Resonance Energy Transfer, Humans, ATP-Binding Cassette Transporters, Electrophoresis, Polyacrylamide Gel, Protein Structure, Quaternary, Dimerization, ATP Binding Cassette Transporter 1, HeLa Cells, Plasmids
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