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J. Biol. Chem., Vol. 276, Issue 35, 32427-32436, August 31, 2001
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From the The bullous pemphigoid
antigen 1 (eBPAG1) is a constituent of hemidesmosomes (HDs),
cell-substrate adhesion complexes in stratified epithelia. Although its
COOH terminus interacts with intermediate filaments, its
NH2 terminus is important for its recruitment into HDs. To identify proteins that interact with the NH2
terminus of human eBPAG1, we performed a yeast two-hybrid screen, which uncovered a protein belonging to the LAP/LERP (for LRR
and PDZ domain) protein family with 16 NH2-terminal leucine-rich repeats and a COOH-terminal PDZ
domain. The gene for this LAP/LERP protein comprises at least 26 exons
located on the long arm of chromosome 5. In most human tissues,
several transcripts were detected differing in the coding region
situated upstream of or within the PDZ domain. One of the encoded
variants was found to correspond to the recently described protein
ERBIN. In yeast and in vitro binding experiments, ERBIN was
shown to interact not only with eBPAG1 but also with the COOH-terminal
region of the cytoplasmic domain of the integrin The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF276423.
The Hemidesmosomal Protein Bullous Pemphigoid Antigen 1 and the
Integrin
4 Subunit Bind to ERBIN
MOLECULAR CLONING OF MULTIPLE ALTERNATIVE SPLICE VARIANTS OF
ERBIN AND ANALYSIS OF THEIR TISSUE EXPRESSION*
§¶,§,
,,,,, and**
Department of Dermatology, University
Medical School, 1211 Geneva 14, Switzerland and the Division of
Cell Biology, The Netherlands Cancer Institute, 1066 CX
Amsterdam, The Netherlands
4 subunit, another
component of HDs. Antibodies raised against the COOH terminus
showed that ERBIN is expressed in keratinocytes. In transfected
epithelial cells the protein, however, was not localized in HDs but was
either diffusely distributed over the cytoplasm or concentrated at the
basolateral plasma membrane. Because ERBIN had been shown previously to
interact with the transmembrane tyrosine kinase receptor Erb-B2, which
in turn associates with the integrin 4 subunit, we suggest that
ERBIN provides a link between HD assembly and Erb-B2 receptor signaling.
*
This work was supported by Swiss National Foundation of
Scientific Research Grants 32-51083.97 and 32-56727.99, Fondation Touraine (Paris), Telethon Action Suisse (Aubonne) (to L. B.), the
Dystrophic Epidermolysis Bullosa Research Association (United Kingdom),
and Dutch Cancer Society Grant NKI 99-2039 (to A. S.).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.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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