@article{b660d6d0596d11dd8d9f000ea68e967b,
title = "Syndecan-4 associates with alpha-actinin.",
abstract = "Cell adhesion to the extracellular matrix influences many cellular functions. The integrin family of matrix receptors plays major roles in the formation of adhesions, but other proteins modulate integrin signaling. Syndecan-4, a transmembrane proteoglycan, cooperatively signals with integrins during the formation of focal adhesions. To date, a direct link between syndecan-4 and the cytoskeleton has remained elusive. We now demonstrate by Triton X-100 extraction immunoprecipitation and in vitro binding assays that the focal adhesion component alpha-actinin interacts with syndecan-4 in a beta-integrin-independent manner.",
author = "Greene, {Daniel K} and Sarka Tumova and Couchman, {John R} and Anne Woods",
note = "Keywords: Actinin; Amino Acid Sequence; Animals; Cell Adhesion; Cells, Cultured; Cytoskeleton; Detergents; Humans; Membrane Glycoproteins; Microscopy, Fluorescence; Molecular Sequence Data; Octoxynol; Precipitin Tests; Protein Binding; Protein Kinase C; Protein Kinase C-alpha; Protein Structure, Tertiary; Proteoglycans; Rats; Sequence Homology, Amino Acid; Syndecan-4",
year = "2002",
doi = "10.1074/jbc.M207123200",
language = "English",
volume = "278",
pages = "7617--23",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "9",
}