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J. Biol. Chem., Vol. 280, Issue 52, 42831-42840, December 30, 2005

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Phosphoinositide Specificity of and Mechanism of Lipid Domain Formation by Annexin A2-p11 Heterotetramer^*

Nikhil A. Gokhale, Alexandra Abraham, Michelle A. Digman, Enrico Gratton, and Wonhwa Cho1

From the Department of Chemistry, University of Illinois, Chicago, Illinois 60607-7061 and the Department of Physics, University of Illinois, Urbana, Illinois 61801-3080

Annexin A2 is a phospholipid-binding protein that forms a heterotetramer (annexin II-p11 heterotetramer; A2t) with p11 (S100A10). It has been reported that annexin A2 is involved in binding to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P₂) and in inducing membrane microdomain formation. To understand the mechanisms underlying these findings, we determined the membrane binding properties of annexin A2 wild type and mutants both as monomer and as A2t. Our results from surface plasmon resonance analysis showed that A2t and annexin A2 has modest selectivity for PtdIns(4,5)P₂ over other phosphoinositides, which is conferred by conserved basic residues, including Lys²⁷⁹ and Lys²⁸¹, on the convex surface of annexin A2. Fluorescence microscopy measurements using giant unilamellar vesicles showed that A2t of wild type, but not (K279A)₂-(p11)₂ or (K281A)₂-(p11)₂, specifically induced the formation of 1-µm-sized PtdIns(4,5)P₂ clusters, which were stabilized by cholesterol. Collectively, these studies elucidate the structural determinant of the PtdIns(4,5)P₂ selectivity of A2t and suggest that A2t may be involved in the regulation of PtdIns(4,5)P₂ clustering in the cell.

Received for publication, July 25, 2005 , and in revised form, September 29, 2005.

^* This work was supported by National Institutes of Health Grants GM52598 and GM68849 (to W. C.) and P41-RRO3155 (to E. G.). 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 To whom correspondence should be addressed: Dept. of Chemistry (M/C 111), University of Illinois, 845 W. Taylor St., Chicago, IL 60607-7061. Tel.: 312-996-4883; Fax: 312-996-2183; E-mail: wcho{at}uic.edu.

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