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J. Biol. Chem., Vol. 279, Issue 12, 10872-10882, March 19, 2004

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Novel Organization and Properties of Annexin 2-Membrane Complexes^*

Olivier Lambert, Nükhet Cavusoglu¶, Jacques Gallay||, Michel Vincent||, Jean Louis Rigaud, Jean-Pierre Henry**, and Jesus Ayala-Sanmartin**

From the ^**Unité de Biologie Cellulaire et Moléculaire de la Sécrétion, CNRS UPR 1929, Institut de Biologie Physico-Chimique, 75005 Paris, Institut Curie, CNRS, 75005 Paris, ^||Laboratoire pour l'Utilisation du Rayonnement Electromagnétique, Université Paris Sud, CNRS, 91898 Orsay, ^¶Laboratoire de Physiopathologie Cellulaire et Moléculaire de la Rétine, INSERM U592, Hôpital St. Antoine, 75012 Paris, and Trafic Membranaire et Signalisation dans les Cellules Épithéliales, INSERM U538, CHU St. Antoine, 75012 Paris, France

Annexin 2 belongs to the annexin family of proteins that bind to phospholipid membranes in a Ca²⁺-dependent manner. Here we show that, under mild acidic conditions, annexin 2 binds to and aggregates membranes containing anionic phospholipids, a fact that questions the mechanism of its interaction with membranes via Ca²⁺ bridges only. The H⁺ sensitivity of annexin 2-mediated aggregation is modulated by lipid composition (i.e. cholesterol content). Cryo-electron microscopy of aggregated liposomes revealed that both the monomeric and the tetrameric forms of the protein form bridges between the liposomes at acidic pH. Monomeric annexin 2 induced two different organizations of the membrane junctions. The first resembled that obtained at pH 7 in the presence of Ca²⁺. For the tetramer, the arrangement was different. These bridges seemed more flexible than the Ca²⁺-mediated junctions allowing the invagination of membranes. Time-resolved fluorescence analysis at mild acidic pH and the measurement of Stokes radius revealed that the protein undergoes conformational changes similar to those induced by Ca²⁺. Labeling with the lipophilic probe 3-(trifluoromethyl)-3-(m-[¹²⁵I]iodophenyl)diazirine indicated that the protein has access to the hydrophobic part of the membrane at both acidic pH in the absence of Ca²⁺ and at neutral pH in the presence of Ca²⁺. Models for the membrane interactions of annexin 2 at neutral pH in the presence of Ca²⁺ and at acidic pH are discussed.

Received for publication, December 12, 2003

^* This work was supported by CNRS and INSERM. 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.

Present address: Institut Européen de Chimie et Biologie, 33607 Pessac, France.

To whom correspondence should be addressed: INSERM U538, CHU St. Antoine, 27 Rue Chaligny, 75012 Paris, France. Tel.: 33-1-40-01-13-40; Fax: 33-1-40-01-13-90; E-mail: jayala{at}chusa.jussieu.fr.

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