Syntenin, a PDZ protein that binds syndecan cytoplasmic domains.

The syndecans are transmembrane proteoglycans that place structurally heterogeneous heparan sulfate chains at the cell surface and a highly conserved polypeptide in the cytoplasm. Their versatile heparan sulfate moieties support various processes of molecular recognition, signaling, and trafficking. Here we report the identification of a protein that binds to the ...
cytoplasmic domains of the syndecans in yeast two-hybrid screens, surface plasmon resonance experiments, and ligand-overlay assays. This protein, syntenin, contains a tandem repeat of PDZ domains that reacts with the FYA C-terminal amino acid sequence of the syndecans. Recombinant enhanced green fluorescent protein (eGFP)-syntenin fusion proteins decorate the plasmamembrane and intracellular vesicles, where they colocalize and cosegregate with syndecans. Cells that overexpress eGFP-syntenin show numerous cell surface extensions, suggesting effects of syntenin on cytoskeleton-membrane organization. We propose that syntenin may function as an adaptor that couples syndecans to cytoskeletal proteins or cytosolic downstream signal-effectors.
Mesh Terms:
Amino Acid Sequence, Animals, Binding Sites, CHO Cells, Carrier Proteins, Cell Membrane, Cricetinae, Cytoskeleton, Humans, Intracellular Signaling Peptides and Proteins, Membrane Glycoproteins, Membrane Proteins, Mice, Microscopy, Fluorescence, Molecular Sequence Data, Protein Binding, Proteoglycans, Recombinant Proteins, Saccharomyces cerevisiae, Sequence Homology, Amino Acid, Syndecan-2, Syntenins
Proc. Natl. Acad. Sci. U.S.A.
Date: Dec. 09, 1997
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