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J. Biol. Chem., Vol. 282, Issue 36, 26552-26561, September 7, 2007

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Ankyrin-G Is a Molecular Partner of E-cadherin in Epithelial Cells and Early Embryos^*

Krishnakumar Kizhatil, Jonathan Q. Davis, Lydia Davis, Jan Hoffman, Brigid L. M. Hogan, and Vann Bennett^¶||1

From the Howard Hughes Medical Institute and Departments of Cell Biology, ^¶Biochemistry, and ^||Neurobiology, Duke University Medical Center, Durham, North Carolina 27710

E-cadherin is a ubiquitous component of lateral membranes in epithelial tissues and is required to form the first lateral membrane domains in development. Here, we identify ankyrin-G as a molecular partner of E-cadherin and demonstrate that ankyrin-G and -2-spectrin are required for accumulation of E-cadherin at the lateral membrane in both epithelial cells and early embryos. Ankyrin-G binds to the cytoplasmic domain of E-cadherin at a conserved site distinct from that of -catenin. Ankyrin-G also recruits -2-spectrin to E-cadherin--catenin complexes, thus providing a direct connection between E-cadherin and the spectrin/actin skeleton. In addition to restricting the membrane mobility of E-cadherin, ankyrin-G and -2-spectrin also are required for exit of E-cadherin from the trans-Golgi network in a microtubule-dependent pathway. Ankyrin-G and -2-spectrin co-localize with E-cadherin in preimplantation mouse embryos. Moreover, knockdown of either ankyrin-G or -2-spectrin in one cell of a two-cell embryo blocks accumulation of E-cadherin at sites of cell-cell contact. E-cadherin thus requires both ankyrin-G and -2-spectrin for its cellular localization in early embryos as well as cultured epithelial cells. We have recently reported that ankyrin-G and -2-spectrin collaborate in biogenesis of the lateral membrane ( Kizhatil, K., Yoon, W., Mohler, P. J., Davis, L. H., Hoffman, J. A., and Bennett, V. (2007) J. Biol. Chem. 282, 2029-2037[Abstract/Free Full Text] ). Together with the current findings, these data suggest a ankyrin/spectrin-based mechanism for coordinating membrane assembly with extracellular interactions of E-cadherin at sites of cell-cell contact.

Received for publication, April 13, 2007 , and in revised form, May 31, 2007.

^* This work was supported by the Howard Hughes Medical Institute and a gift from Johnson and Johnson. 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.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1-S3.

¹ To whom correspondence should be addressed: Howard Hughes Medical Institute and Dept. of Cell Biology, Duke University Medical Center, Durham, NC 27710. Tel.: 919-684-3538; Fax: 919-684-3590; E-mail: benne012{at}mc.duke.edu.

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