@article{9ff92cf0596111dd8d9f000ea68e967b,
title = "A conserved NXIP motif is required for cell adhesion properties of the syndecan-4 ectodomain.",
abstract = "Syndecans are cell surface proteoglycans involved in cell adhesion and motility. Syndecan-4 is an important component of focal adhesions and is involved in cytoskeletal reorganization. Previous work has shown that the syndecan-4 ectodomain can support cell attachment. Here, three vertebrate syndecan-4 ectodomains were compared, including that of the zebrafish, and we have demonstrated that the cell binding activity of the syndecan-4 ectodomain is conserved. Cell adhesion to the syndecan-4 ectodomain appears to be a characteristic of mesenchymal cells. Comparison of syndecan-4 ectodomain sequences led to the identification of three conserved regions of sequence, of which the NXIP motif is important for cell binding activity. We have shown that cell adhesion to the syndecan-4 ectodomain involves beta1 integrins in several cell types.",
author = "Whiteford, {James R} and Couchman, {John R}",
note = "Keywords: 3T3 Cells; Amino Acid Motifs; Amino Acid Sequence; Animals; Breast Neoplasms; COS Cells; Cell Adhesion; Cell Culture Techniques; Cell Line; Cell Line, Tumor; Cercopithecus aethiops; Cloning, Molecular; Conserved Sequence; Cricetinae; Dogs; Endothelial Cells; Female; Fibroblasts; Glutathione Transferase; Humans; Jurkat Cells; K562 Cells; Mice; Molecular Sequence Data; Plasmids; Protein Structure, Tertiary; Rats; Recombinant Fusion Proteins; Sequence Analysis, Protein; Sequence Homology, Amino Acid; Skin; Syndecan-4; Zebrafish",
year = "2006",
doi = "10.1074/jbc.M605553200",
language = "English",
volume = "281",
pages = "32156--63",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "43",
}