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J. Cell Biol.,
Volume 143, Number 5, November 30, 1998 1271-1282
Wellcome/CRC Institute and Department of Anatomy, University of Cambridge, Cambridge CB2 1QR, United Kingdom
Mutations in kakapo were recovered in genetic screens designed to isolate genes required for integrin-mediated adhesion in Drosophila. We cloned the
gene and found that it encodes a large protein (>5,000
amino acids) that is highly similar to plectin and
BPAG1 over the first 1,000-amino acid region, and
contains within this region an 
-actinin type actin-binding domain. A central region containing dystrophin-like
repeats is followed by a carboxy domain that is distinct
from plectin and dystrophin, having neither the intermediate filament-binding domain of plectin nor the
dystroglycan/syntrophin-binding domain of dystrophin. Instead, Kakapo has a carboxy terminus similar to
the growth arrest-specific protein Gas2. Kakapo is
strongly expressed late during embryogenesis at the
most prominent site of position-specific integrin adhesion, the muscle attachment sites. It is concentrated at
apical and basal surfaces of epidermal muscle attachment cells, at the termini of the prominent microtubule bundles, and is required in these cells for strong attachment to muscles. Kakapo is also expressed more widely
at a lower level where it is essential for epidermal cell
layer stability. These results suggest that the Kakapo
protein forms essential links among integrins, actin, and
microtubules.
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