Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1074/jbc.M703158200 on July 9, 2007

J. Biol. Chem., Vol. 282, Issue 36, 26552-26561, September 7, 2007
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Data
Right arrow All Versions of this Article:
282/36/26552    most recent
M703158200v1
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kizhatil, K.
Right arrow Articles by Bennett, V.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kizhatil, K.
Right arrow Articles by Bennett, V.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

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

Krishnakumar Kizhatil{ddagger}§, Jonathan Q. Davis{ddagger}, Lydia Davis{ddagger}, Jan Hoffman{ddagger}, Brigid L. M. Hogan§, and Vann Bennett{ddagger}§||1

From the {ddagger}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 beta-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 beta-catenin. Ankyrin-G also recruits beta-2-spectrin to E-cadherin-beta-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 beta-2-spectrin also are required for exit of E-cadherin from the trans-Golgi network in a microtubule-dependent pathway. Ankyrin-G and beta-2-spectrin co-localize with E-cadherin in preimplantation mouse embryos. Moreover, knockdown of either ankyrin-G or beta-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 beta-2-spectrin for its cellular localization in early embryos as well as cultured epithelial cells. We have recently reported that ankyrin-G and beta-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.

Formula 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.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
ScienceHome page
K. Kizhatil, S. A. Baker, V. Y. Arshavsky, and V. Bennett
Ankyrin-G Promotes Cyclic Nucleotide-Gated Channel Transport to Rod Photoreceptor Sensory Cilia
Science, March 20, 2009; 323(5921): 1614 - 1617.
[Abstract] [Full Text] [PDF]


Home page
JCBHome page
V. Bennett and J. Healy
Being there: cellular targeting of voltage-gated sodium channels in the heart
J. Cell Biol., January 10, 2008; 180(1): 13 - 15.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2007 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement