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Vol. 12, Issue 2, 339-350, February 2001
Laboratory for Glycobiology and Developmental Genetics, Center for
Human Genetics, University of Leuven and Flanders Interuniversity
Institute for Biotechnology, Leuven, B-3000 Belgium
Syntenin is a PDZ protein that binds the cytoplasmic C-terminal FYA
motif of the syndecans. Syntenin is widely expressed. In cell
fractionation experiments, syntenin partitions between the cytosol and
microsomes. Immunofluorescence microscopy localizes endogenous and
epitope-tagged syntenin to cell adhesion sites, microfilaments, and the
nucleus. Syntenin is composed of at least three domains. Both PDZ
domains of syntenin are necessary to target reporter tags to the plasma
membrane. The addition of a segment of 10 amino acids from the
N-terminal domain of syntenin to these PDZ domains increases the
localization of the tags to stress fibers and induces the formation of
long, branching plasma membrane extensions. The addition of the
complete N-terminal region, in contrast, reduces the localization of
the tags to plasma membrane/adhesion sites and stress fibers, and
reduces the morphotypical effects. Recombinant domains of syntenin with
the highest plasma membrane localization display the lowest nuclear
localization. Syndecan-1, E-cadherin,
-catenin, and
-catenin
colocalize with syntenin at cell-cell contacts in epithelial cells, and
coimmunoprecipitate with syntenin from extracts of these cells. These
results suggest a role for syntenin in the composition of adherens
junctions and the regulation of plasma membrane dynamics, and imply a
potential role for syntenin in nuclear processes.
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