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J. Cell Biol.,
Volume 144, Number 1, January 11, 1999 45-57

* Department of Molecular Biology, Massachusetts General Hospital, Department of Genetics, Harvard Medical School,
Boston, Massachusetts 02114; We describe here the molecular and functional characterization of the Caenorhabditis elegans
unc-97 gene, whose gene product constitutes a novel
component of muscular adherens junctions. UNC-97
and homologues from several other species define the
PINCH family, a family of LIM proteins whose modular composition of five LIM domains implicates them as
potential adapter molecules. unc-97 expression is restricted to tissue types that attach to the hypodermis,
specifically body wall muscles, vulval muscles, and
mechanosensory neurons. In body wall muscles, the
UNC-97 protein colocalizes with the
Department of Zoology, University of British Columbia, Vancouver, British Columbia V6T 1Z4;
and § Department of Biology, University of Utah, Salt Lake City, Utah 84112
-integrin PAT-3
to the focal adhesion-like attachment sites of muscles.
Partial and complete loss-of-function studies demonstrate that UNC-97 affects the structural integrity of the
integrin containing muscle adherens junctions and contributes to the mechanosensory functions of touch neurons. The expression of a Drosophila homologue of
unc-97 in two integrin containing cell types, muscles,
and muscle-attached epidermal cells, suggests that unc-97 function in adherens junction assembly and stability has been conserved across phylogeny. In addition to its
localization to adherens junctions UNC-97 can also be
detected in the nucleus, suggesting multiple functions
for this LIM domain protein.
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