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J. Biol. Chem., Vol. 277, Issue 15, 12906-12914, April 12, 2002
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From the Departments of Erbin is a recently described member of the LAP
(leucine-rich repeat and PDZ
domain) protein family. We used a C-terminally displayed phage peptide
library to identify optimal ligands for the Erbin PDZ domain.
Phage-selected peptides were type 1 PDZ ligands that bound with high
affinity and specificity to the Erbin PDZ domain in vitro.
These peptides most closely resembled the C-terminal PDZ domain-binding
motifs of three p120-related catenins:
The Erbin PDZ Domain Binds with High Affinity and Specificity to
the Carboxyl Termini of
-Catenin and ARVCF*
,
, and**
Molecular Oncology and
¶ Protein Engineering, Genentech, Inc., South San Francisco,
California 94080 and the § Department of Neurology, Center
for Neurologic Disease, Brigham and Women's Hospital and Harvard
Medical School, Boston, Massachusetts 02115
-catenin, ARVCF, and p0071
(DSWV-COOH). Analysis of the interactions of the Erbin PDZ domain with
synthetic peptides matching the C termini of ARVCF or -catenin also
demonstrated specific high affinity binding. We characterized the
interactions between the Erbin PDZ domain and both ARVCF and
-catenin in vitro and in vivo. The Erbin PDZ
domain co-localized and coprecipitated with ARVCF or -catenin
complexed with 
-catenin and E/N-cadherin. Mutagenesis and peptide
competition experiments showed that the association of Erbin with the
cadherin-catenin complex was mediated by the interaction of its PDZ
domain with the C-terminal PDZ domain-binding motifs (DSWV-COOH) of
ARVCF and -catenin. Finally, we showed that endogenous -catenin
and Erbin co-localized in and co-immunoprecipitated from neurons. These
results suggest that -catenin and ARVCF may function to mediate the
association of Erbin with the junctional cadherin-catenin complex. They
also demonstrate that C-terminal phage-display technology can be used
to predict physiologically relevant ligands for PDZ domains.
*
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.
To whom correspondence may be addressed: Dept. of Protein
Engineering, Genentech, Inc., 1 DNA Way, South San Francisco, CA 94080. Tel.: 650-225-1056; Fax: 650-225-3734; E-mail: sidhu@gene.com.
**
To whom correspondence may be addressed: Dept. of Molecular
Oncology, Genentech, Inc., 1 DNA Way, South San Francisco, CA 94080. Tel.: 650-225-1123; Fax: 650-225-6127; E-mail:
larsky@earthlink.net.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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