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J. Biol. Chem., Vol. 282, Issue 36, 26629-26640, September 7, 2007

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The Cell Adhesion Receptor Carcinoembryonic Antigen-related Cell Adhesion Molecule 1 Regulates Nucleocytoplasmic Trafficking of DNA Polymerase -Interacting Protein 38^*

Esther Klaile¹, Mario M. Müller, Christoph Kannicht^¶, Wolfgang Otto, Bernhard B. Singer^||, Werner Reutter, Björn Öbrink², and Lothar Lucka²

From the Institut für Biochemie und Molekularbiologie, Charité, Universitätsmedizin Berlin, Campus Benjamin Franklin, Berlin-Dahlem D-14195, Germany, the ^¶Molecular Biochemistry Department, Octapharma Pre-Clinical Research and Development, Arnimallee 22, Berlin D-14195, Germany, the ^||Institute for Anatomy, University Hospital Essen, Hufelandstrasse 55, Essen D-45147, Germany, and the Department of Cell and Molecular Biology, Medical Nobel Institute, Karolinska Institutet, Stockholm SE-17177, Sweden

The homophilic cell-cell adhesion receptor CEACAM1 (carcinoembryonic antigen-related cell adhesion molecule 1, CD66a) acts as a regulator of contact-dependent cell survival, differentiation, and growth. It is involved in the control of proliferation in hematopoietic and epithelial cells and can act as a tumor suppressor. In this study, we identify DNA polymerase -interacting protein 38 (PDIP38) as a novel binding partner for CEACAM1-L and CEACAM1-S. We show that PDIP38 can occur in the nucleus, in the cytoplasm and at the plasma membrane in NBT-II, IEC18, RBE, and HeLa cells and that the distribution in NBT-II cells is influenced by the confluency of the cells. We also demonstrate that the interaction of CEACAM1 and PDIP38 is of functional importance in NBT-II cells, which co-express the long and the short CEACAM1 isoform. In subconfluent, proliferating NBT-II cells, perturbation of CEACAM1 by antibody clustering induces increased binding to PDIP38 and results in rapid recruitment of PDIP38 to the plasma membrane. The same treatment of confluent, quiescent NBT-II cells leads to a different response, i.e. translocation of PDIP38 to the nucleus. Together, our data show that PDIP38 can shuttle between the cytoplasmic and the nuclear compartments and that its subcellular localization is regulated by CEACAM1, implicating that PDIP38 may constitute a novel downstream target of CEACAM1 signaling.

Received for publication, March 1, 2007 , and in revised form, July 9, 2007.

^* This work was supported by the Deutsche Forschungsgemeinschaft (Grant SFB 366, TP C1), the Sonnenfeld-Stiftung, the Fonds der Chemischen Industrie, the Swedish Research Council (Project 32X-05200), the Swedish Cancer Foundation (Project 4720), the Marianne and Marcus Wallenbergs Stiftelse, and the Karolinska Institutet. 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 and S2.

² Both authors contributed equally to this work.

¹ To whom correspondence should be addressed: Esther Klaile, Dept. of Cell and Molecular Biology, Medical Nobel Institute, Karolinska Institutet, von Eulers väg 3, SE-17177 Stockholm, Sweden. Tel.: +46-8-52487302; Fax: +46-8-301833; E-mail: esther.klaile{at}ki.se.

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