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Originally published In Press as doi:10.1074/jbc.M010032200 on February 5, 2001

J. Biol. Chem., Vol. 276, Issue 18, 15256-15263, May 4, 2001
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The ERBB2/HER2 Receptor Differentially Interacts with ERBIN and PICK1 PSD-95/DLG/ZO-1 Domain Proteins*

Fanny Jaulin-BastardDagger §, Hiroko SaitoDagger §, André Le Bivic||, Vincent Ollendorff**, Sylvie MarchettoDagger , Daniel BirnbaumDagger **, and Jean-Paul BorgDagger Dagger Dagger

From Dagger  U119 INSERM, Molecular Oncology, ** Institut Paoli-Calmettes, 27 boulevard Leï Roure, 13009 Marseille and || Institut de Biologie et du Développement de Marseille, Faculté des Sciences de Luminy, Case 907, 13288 Marseille cedex 09, France

Identification of protein complexes associated with the ERBB2/HER2 receptor may help unravel the mechanisms of its activation and regulation in normal and pathological situations. Interactions between ERBB2/HER2 and Src homology 2 or phosphotyrosine binding domain signaling proteins have been extensively studied. We have identified ERBIN and PICK1 as new binding partners for ERBB2/HER2 that associate with its carboxyl-terminal sequence through a PDZ (PSD-95/DLG/ZO-1) domain. This peptide sequence acts as a dominant retention or targeting basolateral signal for receptors in epithelial cells. ERBIN belongs to the newly described LAP (LRR and PDZ) protein family, whose function is crucial in non vertebrates for epithelial homeostasis. Whereas ERBIN appears to locate ERBB2/HER2 to the basolateral epithelium, PICK1 is thought to be involved in the clustering of receptors. We show here that ERBIN and PICK1 bind to ERBB2/HER2 with different mechanisms, and we propose that these interactions are regulated in cells. Since ERBIN and PICK1 tend to oligomerize, further complexity of protein networks may participate in ERBB2/HER2 functions and specificity.

* This work was supported in part by grants from INSERM, Institute Paoli-Calmettes (to V. O. and D. B.), La Ligue Contre le Cancer (to D. B. and J.-P. B.), Association Recherche Contre le Cancer (to A. L. B.), and La Fondation de France (to J.-P. B.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ These authors participated equally in this work.

Recipient of a Japanese-French fellowship.

Dagger Dagger To whom correspondence should be addressed. Tel.: 33-4-91-75-84-09; Fax: 33-4-91-26-03-64; E-mail: borg@marseille.inserm.fr.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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