Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 285, Issue 19, Pages 14247-14258Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M109.056945
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Funding
- Wellcome Trust [065940]
- Danish National Research Foundation
- Haensch Foundation
- Wilhelm Pedersen Fonden through the Novo Nordisk Fonden
- Department of Biomedical Sciences at the University of Copenhagen
- Molecular Medicine Ph.D. program at the University of Copenhagen
- Medical Research Council UK (MRC)
- Versus Arthritis [19207] Funding Source: researchfish
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Fibroblasts null for the transmembrane proteoglycan, syndecan-4, have an altered actin cytoskeleton, compared with matching wild-type cells. They do not organize alpha-smooth muscle actin into bundles, but will do so when full-length syndecan-4 is re-expressed. This requires the central V region of the core protein cytoplasmic domain, though not interactions with PDZ proteins. A second key requirement is multiple heparan sulfate chains. Mutant syndecan-4 with no chains, or only one chain, failed to restore the wild-type phenotype, whereas those expressing two or three were competent. However, clustering of one-chain syndecan-4 forms with antibodies overcame the block, indicating that valency of interactions with ligands is a key component of syndecan-4 function. Measurements of focal contact/adhesion size and focal adhesion kinase phosphorylation correlated with syndecan-4 status and alpha-smooth muscle actin organization, being reduced where syndecan-4 function was compromised by a lack of multiple heparan sulfate chains.
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