The hemidesmosomal protein bullous pemphigoid antigen 1 and the integrin beta 4 subunit bind to ERBIN. Molecular cloning of multiple alternative splice variants of ERBIN and analysis of their tissue expression.

Details

Serval ID
serval:BIB_76459314E7E1
Type
Article: article from journal or magazin.
Collection
Publications
Title
The hemidesmosomal protein bullous pemphigoid antigen 1 and the integrin beta 4 subunit bind to ERBIN. Molecular cloning of multiple alternative splice variants of ERBIN and analysis of their tissue expression.
Journal
Journal of Biological Chemistry
Author(s)
Favre B., Fontao L., Koster J., Shafaatian R., Jaunin F., Saurat J.H., Sonnenberg A., Borradori L.
ISSN
0021-9258
Publication state
Published
Issued date
08/2001
Peer-reviewed
Oui
Volume
276
Number
35
Pages
32427-32436
Language
english
Abstract
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 NH(2) terminus is important for its recruitment into HDs. To identify proteins that interact with the NH(2) 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 NH(2)-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 beta4 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 beta4 subunit, we suggest that ERBIN provides a link between HD assembly and Erb-B2 receptor signaling.
Keywords
Adaptor Proteins, Signal Transducing, Alternative Splicing, Amino Acid Sequence, Animals, Antigens, CD/chemistry, Antigens, CD/metabolism, Autoantigens/chemistry, Autoantigens/metabolism, Base Sequence, Binding Sites, COS Cells, Carrier Proteins/chemistry, Carrier Proteins/genetics, Cell Line, Cercopithecus aethiops, Chromosome Mapping, Chromosomes, Human, Pair 5, Cloning, Molecular, Collagen/chemistry, Collagen/metabolism, Cytoskeletal Proteins, DNA Primers, Desmosomes/metabolism, Exons, Female, Gene Expression Regulation, Genetic Variation, Humans, Integrin beta4, Male, Molecular Sequence Data, Nerve Tissue Proteins, Non-Fibrillar Collagens, Organ Specificity, Pemphigoid, Bullous/genetics, Rats, Recombinant Proteins/chemistry, Recombinant Proteins/metabolism, Restriction Mapping, Reverse Transcriptase Polymerase Chain Reaction, Saccharomyces cerevisiae, Sequence Deletion, Transcription, Genetic, Transfection, Tumor Cells, Cultured, Urinary Bladder Neoplasms
Pubmed
Web of science
Open Access
Yes
Create date
25/01/2008 17:32
Last modification date
08/05/2019 20:33
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