| First Author | Gopal S | Year | 2010 |
| Journal | J Biol Chem | Volume | 285 |
| Issue | 19 | Pages | 14247-58 |
| PubMed ID | 20154082 | Mgi Jnum | J:164620 |
| Mgi Id | MGI:4834734 | Doi | 10.1074/jbc.M109.056945 |
| Citation | Gopal S, et al. (2010) Heparan sulfate chain valency controls syndecan-4 function in cell adhesion. J Biol Chem 285(19):14247-58 |
| abstractText | 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. |
