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Vol. 11, Issue 1, 277-286, January 2000
Department of Cell and Molecular Biology, Northwestern University
Medical School, Chicago, Illinois 60611
In epidermal cells, the keratin cytoskeleton interacts with the
elements in the basement membrane via a multimolecular junction called
the hemidesmosome. A major component of the hemidesmosome plaque is the
230-kDa bullous pemphigoid autoantigen (BP230/BPAG1), which connects
directly to the keratin-containing intermediate filaments of the
cytoskeleton via its C terminus. A second bullous pemphigoid antigen of
180 kDa (BP180/BPAG2) is a type II transmembrane component of the
hemidesmosome. Using yeast two-hybrid technology and recombinant
proteins, we show that an N-terminal fragment of BP230 can bind
directly to an N-terminal fragment of BP180. We have also explored the
consequences of expression of the BP230 N terminus in 804G cells that
assemble hemidesmosomes in vitro. Unexpectedly, this fragment disrupts
the distribution of BP180 in transfected cells but has no apparent
impact on the organization of endogenous BP230 and 
6
4
integrin. We propose that the BP230 N terminus competes with
endogenous BP230 protein for BP180 binding and inhibits incorporation
of BP180 into the cell surface at the site of the hemidesmosome. These
data provide new insight into those interactions of the molecules of
the hemidesmosome that are necessary for its function in integrating
epithelial and connective tissue types.
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