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A more recent version of this article appeared on May 1, 2003
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Submitted on August 30, 2002
Revised on December 11, 2002
Accepted on December 27, 2002
1 Department of Dermatology, University Hospital, Geneva, Switzerland
2 Department of Dermatology, University Hospital, Geneva, Switzerland (present address: Novartis Forschungsinstitut, IDTA, Wien, Austria)
3 Division of Cell Biology, The Netherlands Cancer Institute, Amsterdam, The Netherlands (present address: Department of Human Genetics, Academic Medical Center, Amsterdam, The Netherlands)
4 Departments of Pathology, Dermatology and the R.H. Lurie Cancer Center, Northwestern University Feinberg School of Medicine, Chicago, USA
5 Division of Cell Biology, The Netherlands Cancer Institute, Amsterdam, The Netherlands
* Corresponding author. E-mail address: luca.borradori{at}hcuge.ch.
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 (IF). 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 8-amino acid stretch. In contrast, the C subdomain with the COOH-terminal extremity of DP interacts with K5/K14 and K8/K18, while 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 only interacted with cytokeratins 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. Based on 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; 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 primarly located in the rod domain of these keratins.
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