Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly

Détails

ID Serval
serval:BIB_CA692B14F871
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly
Périodique
Journal of Cell Science
Auteur(s)
Koster  J., Geerts  D., Favre  B., Borradori  L., Sonnenberg  A.
ISSN
0021-9533 (Print)
Statut éditorial
Publié
Date de publication
01/2003
Volume
116
Numéro
Pt 2
Pages
387-99
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Jan 15
Résumé
Hemidesmosomes (HDs) are multi-protein complexes that promote stable adhesion of epithelial cells to the underlying extracellular matrix. We assessed the interactions between different hemidesmosomal components with each other, mapped the binding sites and studied the importance of these interactions for HD assembly in yeast two-hybrid and cell-transfection assays. The results show that: (1) bullous pemphigoid antigen (BP) 180 binds not only to BP230, but also to plectin. The interactions between these proteins are facilitated by the Y subdomain in the N-terminal plakin domain of BP230 and plectin, and residues 145-230 of the cytoplasmic domain of BP180; (2) different, but overlapping, sequences on BP180 mediate binding to beta4, which, in turn associates with BP180 via its third fibronectin type III repeat; (3) sequences in the N-terminal extremity of BP230 mediate its binding to beta4, which requires the C-terminal end of the connecting segment up to the fourth FNIII repeat of the beta4 subunit. (4) Finally, cell-transfection studies showed that the localization of BP230 into hemidesmosome-like structures depends on its Z-Y subdomains as well as on the availability of BP180. By having further uncovered interactions between various hemidesmosomal components, mapped the involved binding sites and dissected a hierarchy of interactions relevant for their topogenic fate, our findings give novel insights into the molecular organization of hemidesmosomes.
Mots-clé
Autoantigens/genetics/metabolism *Carrier Proteins Cell Adhesion/*physiology Cell Line, Transformed Collagen/genetics/metabolism *Cytoskeletal Proteins Epithelial Cells/cytology/*metabolism Hemidesmosomes/*metabolism Humans Integrin alpha6beta4/genetics/metabolism Intermediate Filament Proteins/genetics/metabolism Keratinocytes/cytology/metabolism Membrane Proteins/*metabolism *Nerve Tissue Proteins *Non-Fibrillar Collagens Pemphigoid, Bullous/genetics/metabolism Plectin Protein Binding/genetics Protein Structure, Tertiary/genetics Transfection Two-Hybrid System Techniques
Pubmed
Web of science
Open Access
Oui
Création de la notice
25/01/2008 17:32
Dernière modification de la notice
09/05/2019 1:14
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