HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 278, Issue 50, 50338-50345, December 12, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/50/50338    most recent M309115200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kirshner, J. Articles by Shively, J. E. Search for Related Content PubMed PubMed Citation Articles by Kirshner, J. Articles by Shively, J. E. Social Bookmarking                      What's this?

CEACAM1, a Cell-Cell Adhesion Molecule, Directly Associates with Annexin II in a Three-dimensional Model of Mammary Morphogenesis^*

Julia Kirshner, Detlef Schumann, and John E. Shively¶

From the Graduate School of the City of Hope and Beckman Research Institute and the Division of Immunology, Beckman Research Institute of the City of Hope, Duarte, California 91010

The epithelial cell adhesion molecule CEACAM1 (carcinoembryonic antigen cell adhesion molecule-1) is down-regulated in colon, prostate, breast, and liver cancer. Here we show that CEACAM1-4S, a splice form with four Ig-like ectodomains and a short cytoplasmic domain (14 amino acids), directly associates with annexin II, a lipid raft-associated molecule, which is also down-regulated in many cancers. Annexin II was identified using a glutathione S-transferase pull-down assay in which the cytoplasmic domain of CEACAM-4S was fused to glutathione S-transferase, the fusion protein was incubated with cell lysates, and isolated proteins were sequenced by mass spectrometry. The interaction was confirmed first by reciprocal immunoprecipitations using anti-CEACAM1 and anti-annexin II antibodies and second by confocal laser microscopy showing co-localization of CEACAM1 with annexin II in mammary epithelial cells grown in Matrigel. In addition, CEACAM1 co-localized with p11, a component of the tetrameric AIIt complex at the plasma membrane, and with annexin II in secretory vesicles. Immobilized, oriented peptides from the cytoplasmic domain of CEACAM1-4S were shown to directly associate with bovine AIIt, which is 98% homologous to human AIIt, with average K_D values of about 30 nM using surface plasmon resonance, demonstrating direct binding of functionally relevant AIIt to the cytoplasmic domain of CEACAM1-4S.

Received for publication, August 18, 2003 , and in revised form, September 28, 2003.

^* This research was supported by National Cancer Institute, National Institutes of Health Grant CA84202. 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. Tel.: 626-359-8111 (ext. 62601); Fax: 626-301-8186; E-mail: jshively{at}coh.org.

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

This article has been cited by other articles:

				L. Jin, Y. Li, C.-J. Chen, M. A. Sherman, K. Le, and J. E. Shively Direct Interaction of Tumor Suppressor CEACAM1 with Beta Catenin: Identification of Key Residues in the Long Cytoplasmic Domain Experimental Biology and Medicine, July 1, 2008; 233(7): 849 - 859. [Abstract] [Full Text] [PDF]

				C.-J. Chen, J. Kirshner, M. A. Sherman, W. Hu, T. Nguyen, and J. E. Shively Mutation Analysis of the Short Cytoplasmic Domain of the Cell-Cell Adhesion Molecule CEACAM1 Identifies Residues That Orchestrate Actin Binding and Lumen Formation J. Biol. Chem., February 23, 2007; 282(8): 5749 - 5760. [Abstract] [Full Text] [PDF]

				E. Klaile, M. M. Muller, C. Kannicht, B. B. Singer, and L. Lucka CEACAM1 functionally interacts with filamin A and exerts a dual role in the regulation of cell migration J. Cell Sci., December 1, 2005; 118(23): 5513 - 5524. [Abstract] [Full Text] [PDF]

				M. M. Muller, B. B. Singer, E. Klaile, B. Obrink, and L. Lucka Transmembrane CEACAM1 affects integrin-dependent signaling and regulates extracellular matrix protein-specific morphology and migration of endothelial cells Blood, May 15, 2005; 105(10): 3925 - 3934. [Abstract] [Full Text] [PDF]

				U. Rescher and V. Gerke Annexins - unique membrane binding proteins with diverse functions J. Cell Sci., June 1, 2004; 117(13): 2631 - 2639. [Abstract] [Full Text] [PDF]