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Journal of Cell Science 116, e203-e203 (2003)
Copyright © 2003 The Company of Biologists Limited


In this issue

Assembling the hemidesmosome


Hemidesmosomes are rivet-like complexes that anchor epithelial cells to the extracellular matrix (ECM), physically linking it to the cell's cytoskeleton. They contain at least five proteins: integrin {alpha}6ß4, which is central to the complex and binds to laminin 5 in the ECM; plectin, a plakin that connects the complex to keratin intermediate filaments; bullous pemphigoid antigen 230 (BP230), another plakin; BP180; and CD151. Arnoud Sonnenberg and co-workers have examined how these components fit together, combining exhaustive two-hybrid analysis with assessment of the ability of point mutants to complement genetic deficiencies in keratinocytes (see p. 387). This has allowed them to map pairwise interactions between the integrin, plectin, BP180 and BP230. The studies also reveal a hierarchical assembly mechanism of unanticipated complexity. For example, although BP230 can interact with both {alpha}6ß4 and BP180, plectin is required for incorporation of BP180, and recruitment of BP230 occurs only if BP180 is present. These findings allow the authors to propose an assembly model in which the integrin first interacts with plectin, which unfolds its cytoplasmic domain, and BP180 and BP230 are then recruited sequentially.


Related articles in JCS:

Analysis of the interactions between BP180, BP230, plectin and the integrin {alpha}6ß4 important for hemidesmosome assembly
Jan Koster, Dirk Geerts, Bertrand Favre, Luca Borradori, and Arnoud Sonnenberg
JCS 2003 116: 387-399. [Abstract] [Full Text]  




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