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A more recent version of this article appeared on January 1, 2004
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Submitted on May 7, 2003
Revised on September 1, 2003
Accepted on September 9, 2003
1 Humangenetik fuer Biologen, Johann Wolfgang Goethe-Universität, Siesmayerstr. 70, D-60054 Frankfurt, Germany
2 Bürgerhospital Frankfurt, Section of Gynecological Endocrinology and Fertility Surgery, Nibelungenallee 37-41, D-60318 Frankfurt, Germany
* Corresponding author. E-mail address: starzinski-powitz{at}em.uni-frankfurt.de.
While searching for potential candidate molecules relevant for the
pathogenesis of endometriosis, we discovered a 2910 base pairs cDNA
encoding a novel putative 411 amino acid integral membrane protein
which we called shrew-1. The putative open-reading frame was confirmed
with antibodies against shrew-1 peptides which labeled a protein of ca.
48 kDa in extracts of shrew-1 mRNA positive tissue and also detected
ectopically expressed shrew-1. Expression of epitope-tagged shrew-1 in
epithelial cells and analysis by surface biotinylation and
immunoblots demonstrated that shrew-1 is indeed a
transmembrane protein. Shrew-1 is able to target to E-cadherin-mediated
adherens junctions and interact with the E-cadherin-catenin complex in
polarised MCF7 and MDCK cells, but not with the N-cadherin-catenin
complex in nonpolarised epithelial cells. Direct interaction of shrew-1
with 
-catenin in in vitro pulldown assay suggests that -catenin
might be one of the proteins that targets and/or retains shrew-1 in the
adherens junctions. Interestingly, shrew-1 was partially translocated
in response to scatter factor (ligand of receptor tyrosine kinase
c-met) from the plasma membrane to the cytoplasm where it still
colocalized with endogenous E-cadherin. In summary, we introduce
shrew-1 as a novel component of adherens junctions, interacting with
E-cadherin--catenin complexes in polarised epithelial cells.
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