Syntenin, a PDZ protein that binds syndecan cytoplasmic domains

作者：Johan Grootjans, Pascale Zimmermann, Gunter Reekmans, An Smets, Gisèle Degeest, Joachim Dürr, Guido David · 发表于：Proceedings of the National Academy of Sciences · 年份：1997 · DOI：10.1073/pnas.94.25.13683 · 被引用次数：425 · 研究领域：Hippo pathway signaling and YAP/TAZ、Wnt/β-catenin signaling in development and cancer、Proteoglycans and glycosaminoglycans research

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.