The ERBB2/HER2 Receptor Differentially Interacts with ERBIN and PICK1 PSD-95/DLG/ZO-1 Domain Proteins

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 extens...

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Bibliographic Details
Published in:The Journal of biological chemistry 2001-05, Vol.276 (18), p.15256-15263
Main Authors: Jaulin-Bastard, Fanny, Saito, Hiroko, Le Bivic, André, Ollendorff, Vincent, Marchetto, Sylvie, Birnbaum, Daniel, Borg, Jean-Paul
Format: Article
Language:English
Subjects:
Adaptor Proteins, Signal Transducing
Amino Acid Sequence
Animals
Binding Sites
Carrier Proteins - chemistry
Carrier Proteins - metabolism
Cell Line
Discs Large Homolog 1 Protein
Disks Large Homolog 4 Protein
Guanylate Kinases
Humans
Intracellular Signaling Peptides and Proteins
Life Sciences
Membrane Proteins - metabolism
Molecular Sequence Data
Nerve Tissue Proteins - metabolism
Nuclear Proteins - metabolism
Phosphoproteins - metabolism
Protein Binding
Proteins - metabolism
Receptor, ErbB-2 - metabolism
Sequence Homology, Amino Acid
Two-Hybrid System Techniques
Zonula Occludens-1 Protein
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M010032200