Control of morphology, cytoskeleton and migration by syndecan-4.

Publisher: Company of Biologists Country of Publication: England NLM ID: 0052457 Publication Model: Print Cited Medium: Print ISSN: 0021-9533 (Print) Linking ISSN: 00219533 NLM ISO Abbreviation: J Cell Sci Subsets: MEDLINE

Publication: Cambridge : Company of Biologists
Original Publication: London.

Membrane Glycoproteins/*physiology ; Proteoglycans/*physiology; Amino Acid Sequence ; Animals ; CHO Cells ; Cell Adhesion/physiology ; Cell Division ; Cell Size ; Chemotaxis ; Cricetinae ; Cytoskeleton/physiology ; Cytoskeleton/ultrastructure ; Epithelial Cells/cytology ; Epithelial Cells/physiology ; Flow Cytometry ; Liver/metabolism ; Membrane Glycoproteins/chemistry ; Membrane Glycoproteins/genetics ; Molecular Sequence Data ; Mutagenesis ; Protein Kinase C/metabolism ; Proteoglycans/chemistry ; Proteoglycans/genetics ; Rats ; Recombinant Proteins/metabolism ; Sequence Deletion ; Sequence Homology, Amino Acid ; Syndecan-2 ; Syndecan-4 ; Transfection

Syndecan-4 is a widely expressed transmembrane heparan sulfate proteoglycan which localizes to focal adhesions. Previous studies showed that the syndecan-4 cytoplasmic domain can associate with and potentiate the activity of protein kinase C, which is required for focal adhesion formation. To examine further the role of syndecan-4 in cell adhesion, we expressed syndecan-4 cDNA constructs in CHO-K1 cells. Syndecan-2 transfection was used to confirm effects seen were specific for syndecan-4. Cells overexpressing full length syndecan-4 core protein exhibited a more flattened, fibroblastic morphology, with increased focal adhesion formation and decreased cell motility. Expression of a syndecan-4 core protein with either a partial or complete deletion of the cytoplasmic domain or of an antisense construct led to markedly decreased spreading and focal adhesion formation, a more epithelioid morphology, and decreased motility. Overexpression of syndecan-2 changed the adhesive phenotype, but did not markedly alter focal adhesion and microfilament bundle formation. The data suggest that syndecan-4 is a regulator of focal adhesion and stress fiber formation, and influences both morphology and migration.

Comment in: J Cell Sci. 1999 Oct;112 ( Pt 20):3415-20. (PMID: 10504290)

GM50194 United States GM NIGMS NIH HHS

0 (Membrane Glycoproteins)
0 (Proteoglycans)
0 (Recombinant Proteins)
0 (Sdc2 protein, rat)
0 (Sdc4 protein, rat)
0 (Syndecan-4)
149769-25-5 (Syndecan-2)
EC 2.7.11.13 (Protein Kinase C)

Date Created: 19991003 Date Completed: 20000110 Latest Revision: 20220215

20231215

10.1242/jcs.112.20.3421

10504291