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J. Biol. Chem., Vol. 281, Issue 29, 20283-20290, July 21, 2006

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Transition from Dimers to Higher Oligomeric Forms Occurs during the ATPase Cycle of the ABCA1 Transporter^*

From the Centre d'Immunologie de Marseille-Luminy INSERM CNRS UniversitédelaMéditerranée, Parc Scientifique de Luminy, 13288 Marseille Cedex 09 France

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.

Received for publication, February 3, 2006 , and in revised form, May 4, 2006.

^* This work was supported in part by institutional grants from INSERM and CNRS and specific grants from the European Community. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement"in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Funded in part by a fellowship allocated by the Nouvelle Société Française d'Athérosclérose/Fournier Pharma.

² To whom correspondence should be addressed: Centre d'Immunologie de Marseille-Luminy INSERM CNRS Université delaMéditerranée, Parc Scientifique de Luminy, Case 906, 13288 Marseille Cedex 09 France. Tel.: 33-4-91269404; Fax: 33-4-91269430; E-mail: chimini{at}ciml.univ-mrs.fr.

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