Transition from dimers to higher oligomeric forms occurs during the ATPase cycle of the ABCA1 transporter.
J Biol Chem
; 281(29): 20283-90, 2006 Jul 21.
Article
em En
| MEDLINE
| ID: mdl-16709568
ABSTRACT
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.
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Base de dados:
MEDLINE
Assunto principal:
Adenosina Trifosfatases
/
Transportadores de Cassetes de Ligação de ATP
Idioma:
En
Ano de publicação:
2006
Tipo de documento:
Article