Syndecan-2 is a novel ligand for the protein tyrosine phosphatase receptor CD148
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Syndecan-2 is a heparan sulfate proteoglycan that has a cell adhesion regulatory domain contained within its extracellular core protein. Cell adhesion to the syndecan-2 extracellular domain (S2ED) is ß1 integrin dependent; however, syndecan-2 is not an integrin ligand. Here the protein tyrosine phosphatase receptor CD148 is shown to be a key intermediary in cell adhesion to S2ED, with downstream ß1 integrin-mediated adhesion and cytoskeletal organization. We show that S2ED is a novel ligand for CD148 and identify the region proximal to the transmembrane domain of syndecan-2 as the site of interaction with CD148. A mechanism for the transduction of the signal from CD148 to ß1 integrins is elucidated requiring Src kinase and potential implication of the C2ß isoform of phosphatidylinositol 3 kinase. Our data uncover a novel pathway for ß1 integrin-mediated adhesion of importance in cellular processes such as angiogenesis and inflammation.
|Journal||Molecular Biology of the Cell|
|Number of pages||16|
|Publication status||Published - 2011|
- Animals, Antigens, CD29, Cell Adhesion, Cell Line, Cytoskeleton, Fibroblasts, Gene Expression Regulation, Humans, Inflammation, Jurkat Cells, Ligands, Lung, Mice, Neovascularization, Physiologic, Phosphatidylinositol 3-Kinase, Protein Interaction Domains and Motifs, RNA, Small Interfering, Rats, Receptor-Like Protein Tyrosine Phosphatases, Class 3, Signal Transduction, Syndecan-2, src-Family Kinases