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J. Cell Biol.,
Volume 144, Number 3, February 8, 1999 435-446
* Departments of Biochemistry and Molecular Biophysics and The dystonia musculorum (dt) mouse suffers
from severe degeneration of primary sensory neurons.
The mutated gene product is named dystonin and is
identical to the neuronal isoform of bullous pemphigoid antigen 1 (BPAG1-n). BPAG1-n contains an actin-binding domain at its NH2 terminus and a putative
intermediate filament-binding domain at its COOH
terminus. Because the degenerating sensory neurons of
dt mice display abnormal accumulations of intermediate filaments in the axons, BPAG1-n has been postulated to organize the neuronal cytoskeleton by interacting with both the neurofilament triplet proteins
(NFTPs) and microfilaments. In this paper we show by
a variety of methods that the COOH-terminal tail domain of mouse BPAG1 interacts specifically with peripherin, but in contrast to a previous study (Yang, Y.,
J. Dowling, Q.C. Yu, P. Kouklis, D.W. Cleveland, and
E. Fuchs. 1996. Cell. 86:655-665), mouse BPAG1 fails
to associate with full-length NFTPs. The tail domains
interfered with the association of the NFTPs with
BPAG1. In dt mice, peripherin is present in axonal
swellings of degenerating sensory neurons in the dorsal
root ganglia and is downregulated even in other neural
regions, which have no obvious signs of pathology. Since peripherin and BPAG1-n also display similar expression patterns in the nervous system, we suggest that
peripherin is the specific interaction partner of
BPAG1-n in vivo.
Departments of Pathology and Anatomy and Cell Biology,
Columbia University College of Physicians and Surgeons, New York 10032
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