Interaction of the bullous pemphigoid antigen 1 (BP230) and desmoplakin with intermediate filaments is mediated by distinct sequences within their COOH terminus

Détails

ID Serval
serval:BIB_2BED6B2A0D53
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Interaction of the bullous pemphigoid antigen 1 (BP230) and desmoplakin with intermediate filaments is mediated by distinct sequences within their COOH terminus
Périodique
Molecular Biology of the Cell
Auteur(s)
Fontao  L., Favre  B., Riou  S., Geerts  D., Jaunin  F., Saurat  J. H., Green  K. J., Sonnenberg  A., Borradori  L.
ISSN
1059-1524 (Print)
Statut éditorial
Publié
Date de publication
05/2003
Volume
14
Numéro
5
Pages
1978-92
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: May
Résumé
The bullous pemphigoid antigen 1 (BP230) and desmoplakin (DP) are members of the plakin protein family of cytolinkers. Despite their homology, their COOH termini selectively bind distinct intermediate filaments (IFs). We studied sequences within their COOH termini required for their interaction with the epidermal keratins K5/K14, the simple epithelial keratins K8/K18, and type III IF vimentin by yeast three-hybrid, cell transfection, and overlay assays. The results indicate that BP230 interacts with K5/K14 but not with K8/K18 or vimentin via a region encompassing both the B and C subdomains and the COOH extremity, including a COOH-terminal eight-amino-acid stretch. In contrast, the C subdomain with the COOH-terminal extremity of DP interacts with K5/K14 and K8/K18, and its linker region is able to associate with K8/K18 and vimentin. Furthermore, the potential of DP to interact with IF proteins in yeast seems to be regulated by phosphorylation of Ser 2849 within its COOH terminus. Strikingly, BP230 and DP interacted with cytokeratins only when both type I and type II keratins were present. The head and tail domains of K5/K14 keratins were dispensable for their interaction with BP230 or DP. On the basis of our findings, we postulate that (1) the binding specificity of plakins for various IF proteins depends on their linker region between the highly homologous B and C subdomains and their COOH extremity and (2) the association of DP and BP230 with both epidermal and simple keratins is critically affected by the tertiary structure induced by heterodimerization and involves recognition sites located primarily in the rod domain of these keratins.
Mots-clé
Amino Acid Sequence Animals Autoantigens/*metabolism COS Cells *Carrier Proteins Collagen/*metabolism Cytoskeletal Proteins/*metabolism Desmoplakins Dimerization Immunoblotting Intermediate Filaments/*metabolism Keratin-14 Keratin-5 Keratins/metabolism Molecular Sequence Data *Nerve Tissue Proteins *Non-Fibrillar Collagens Serine/metabolism Two-Hybrid System Techniques
Pubmed
Web of science
Création de la notice
25/01/2008 17:32
Dernière modification de la notice
03/03/2018 15:26
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