Syndecan-4 associates with alpha-actinin.

Research output: Contribution to journalJournal articleResearchpeer-review

Daniel K Greene, Sarka Tumova, John R Couchman, Anne Woods

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.
Original languageEnglish
JournalJournal of Biological Chemistry
Volume278
Issue number9
Pages (from-to)7617-23
Number of pages6
ISSN0021-9258
DOIs
Publication statusPublished - 2002

Bibliographical 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

ID: 5162703