ERBIN: a basolateral PDZ protein that interacts with the mammalian ERBB2/HER2 receptor

The ERBB receptors have a crucial role in morphogenesis and oncogenesis. We have identified a new PDZ protein we named ERBIN (ERBB2 interacting protein) that acts as an adaptor for the receptor ERBB2/HER2 in epithelia. ERBIN contains 16 leucine-rich repeats (LRRs) in its amino terminus and a PDZ (PS...

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Bibliographic Details
Published in:	Nature cell biology 2000-07, Vol.2 (7), p.407-414
Main Authors:	Borg, Jean-Paul, Marchetto, Sylvie, Le Bivic, André, Ollendorff, Vincent, Jaulin-Bastard, Fanny, Saito, Hiroko, Fournier, Emmanuel, Adélaïde, José, Margolis, Ben, Birnbaum, Daniel
Format:	Article
Language:	eng
Subjects:	Adaptor Proteins, Signal Transducing Amino Acid Sequence Animals Binding Sites Biological Transport Caco-2 Cells Carrier Proteins - metabolism Cell Line Cell Membrane - chemistry Cell Membrane - metabolism Cell Polarity Dogs Enzyme Activation Epidermal growth factor Epithelial Cells - chemistry Epithelial Cells - cytology Epithelial Cells - metabolism Fluorescent Antibody Technique Humans Intestines - cytology Kidney - metabolism Kinases Life Sciences Ligands Localization Mice Molecular Sequence Data Mutation Phosphorylation Protein Binding Protein Structure, Tertiary Protein-protein interactions Proteins Receptor, ErbB-2 - metabolism RNA, Messenger - analysis RNA, Messenger - genetics Sequence Alignment Substrate Specificity Two-Hybrid System Techniques
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Summary:	The ERBB receptors have a crucial role in morphogenesis and oncogenesis. We have identified a new PDZ protein we named ERBIN (ERBB2 interacting protein) that acts as an adaptor for the receptor ERBB2/HER2 in epithelia. ERBIN contains 16 leucine-rich repeats (LRRs) in its amino terminus and a PDZ (PSD-95/DLG/ZO-1) domain at its carboxy terminus, and belongs to a new PDZ protein family. The PDZ domain directly and specifically interacts with ERBB2/HER2. ERBIN and ERBB2/HER2 colocalize to the lateral membrane of human intestinal epithelial cells. The ERBIN-binding site in ERBB2/HER2 has a critical role in restricting this receptor to the basolateral membrane of epithelial cells, as mutation of the ERBIN-binding site leads to the mislocalization of the receptor in these cells. We suggest that ERBIN acts in the localization and signalling of ERBB2/HER2 in epithelia.
ISSN:	1465-7392 1476-4679