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J. Biol. Chem., Vol. 280, Issue 5, 3747-3756, February 4, 2005

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The Tight Junction Protein Occludin and the Adherens Junction Protein -Catenin Share a Common Interaction Mechanism with ZO-1^*

Sebastian L. Müller, Michael Portwich, Anke Schmidt, Darkhan I. Utepbergenov, Otmar Huber¶, Ingolf E. Blasig, and Gerd Krause||

From the Forschungsinstitut für Molekulare Pharmakologie, 13125 Berlin, Charité-Campus Mitte, 10117 Berlin, Germany, and ^¶Charité-Campus Benjamin Franklin, 12203 Berlin, Germany

The exact sites, structures, and molecular mechanisms of interaction between junction organizing zona occludence protein 1 (ZO-1) and the tight junction protein occludin or the adherens junction protein -catenin are unknown. Binding studies by surface plasmon resonance spectroscopy and peptide mapping combined with comparative modeling utilizing crystal structures led for the first time to a molecular model revealing the binding of both occludin and -catenin to the same binding site in ZO-1. Our data support a concept that ZO-1 successively associates with -catenin at the adherens junction and occludin at the tight junction. Strong spatial evidence indicates that the occludin C-terminal coiled-coil domain dimerizes and interacts finally as a four-helix bundle with the identified structural motifs in ZO-1. The helix bundle of occludin^406–521 and -catenin^509–906 interacts with the hinge region (ZO-1^591–632 and ZO-1^591–622, respectively) and with (ZO-1^726–754 and ZO-1^756–781) in the GuK domain of ZO-1 containing coiled-coil and -helical structures, respectively. The selectivity of both protein-protein interactions is defined by complementary shapes and charges between the participating epitopes. In conclusion, a common molecular mechanism of forming an intermolecular helical bundle between the hinge region/GuK domain of ZO-1 and -catenin and occludin is identified as a general molecular principle organizing the association of ZO-1 at adherens and tight junctions.

Received for publication, October 5, 2004 , and in revised form, November 15, 2004.

^* This work was supported by Deutsche Forschungsgemeinschaft Grant DFG BL308/6. 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.

^|| To whom correspondence should be addressed: Forschungsinstitut für molekulare Pharmakologie, Robert-Rössle-Strasse 10, 13125 Berlin, Germany. Tel.: 49-30-94793228; Fax: 49-30-94793230; E-mail: gkrause{at}fmp-berlin.de.

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