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Review
. 2000 May 29;149(5):995-8.
doi: 10.1083/jcb.149.5.995.

Syndecan-regulated receptor signaling

A C Rapraeger  1
Affiliations
Review

Syndecan-regulated receptor signaling

A C Rapraeger. J Cell Biol. .
No abstract available

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Figures

Figure 1
Figure 1
Syndecan functional domains. The extracellular, transmembrane and cytoplasmic domains of the syndecans contain important features, but the exact roles of these regions and how their function may be regulated remains uncertain.
Figure 2
Figure 2
Syndecan-regulated signaling. Speculative examples of signaling mechanisms regulated by syndecans. (A) Cell–cell adhesion. Syndecan localized to sites of cell–cell adhesion (epithelial adherens junctions, neuronal synapses) may regulate the distribution of cytoskeletal/nuclear proteins CASK, protein 4.1 and β-catenin. (B) Signaling by HS-binding growth factors. Syndecan HS binds growth factors (GF) and growth factor receptors, regulating their assembly (positively or negatively) into signaling complexes. (C) Cell–matrix adhesion. Syndecans (syndecan-4) participate with integrins in focal adhesion assembly. Here, binding to ADAM 12 (step 1) may trigger syndecan core protein interactions with β1 integrins or unidentified signaling partners, leading to integrin activation. Alternatively, HS binding to the ADAM 12-cys region (CR) may alter CR domain conformation (step 2), exposing a cryptic binding site for β1 integrin binding and activation. This activation leads to focal adhesion and stress fiber formation, suggesting the participation of syndecan-4 and its associated syndesmos (Syn) and protein kinase C-α (PKC). DI, disintegrin domain; MP, metalloproteinase domain; FAK, focal adhesion kinase).
Figure 2
Figure 2
Syndecan-regulated signaling. Speculative examples of signaling mechanisms regulated by syndecans. (A) Cell–cell adhesion. Syndecan localized to sites of cell–cell adhesion (epithelial adherens junctions, neuronal synapses) may regulate the distribution of cytoskeletal/nuclear proteins CASK, protein 4.1 and β-catenin. (B) Signaling by HS-binding growth factors. Syndecan HS binds growth factors (GF) and growth factor receptors, regulating their assembly (positively or negatively) into signaling complexes. (C) Cell–matrix adhesion. Syndecans (syndecan-4) participate with integrins in focal adhesion assembly. Here, binding to ADAM 12 (step 1) may trigger syndecan core protein interactions with β1 integrins or unidentified signaling partners, leading to integrin activation. Alternatively, HS binding to the ADAM 12-cys region (CR) may alter CR domain conformation (step 2), exposing a cryptic binding site for β1 integrin binding and activation. This activation leads to focal adhesion and stress fiber formation, suggesting the participation of syndecan-4 and its associated syndesmos (Syn) and protein kinase C-α (PKC). DI, disintegrin domain; MP, metalloproteinase domain; FAK, focal adhesion kinase).
Figure 2
Figure 2
Syndecan-regulated signaling. Speculative examples of signaling mechanisms regulated by syndecans. (A) Cell–cell adhesion. Syndecan localized to sites of cell–cell adhesion (epithelial adherens junctions, neuronal synapses) may regulate the distribution of cytoskeletal/nuclear proteins CASK, protein 4.1 and β-catenin. (B) Signaling by HS-binding growth factors. Syndecan HS binds growth factors (GF) and growth factor receptors, regulating their assembly (positively or negatively) into signaling complexes. (C) Cell–matrix adhesion. Syndecans (syndecan-4) participate with integrins in focal adhesion assembly. Here, binding to ADAM 12 (step 1) may trigger syndecan core protein interactions with β1 integrins or unidentified signaling partners, leading to integrin activation. Alternatively, HS binding to the ADAM 12-cys region (CR) may alter CR domain conformation (step 2), exposing a cryptic binding site for β1 integrin binding and activation. This activation leads to focal adhesion and stress fiber formation, suggesting the participation of syndecan-4 and its associated syndesmos (Syn) and protein kinase C-α (PKC). DI, disintegrin domain; MP, metalloproteinase domain; FAK, focal adhesion kinase).
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References

    1. Baciu P.C., Saoncella S., Lee S.H., Denhez F., Leuthardt D., Goetinck P.F. Syndesmos, a protein that interacts with the cytoplasmic domain of syndecan-4, mediates cell spreading and actin cytoskeletal organization. J. Cell Sci. 2000;113:315–324. - PubMed
    1. Bernfield M., Gotte M., Park P.W., Reizes O., Fitzgerald M.L., Lincecum J., Zako M. Functions of cell surface heparan sulfate proteoglycans. Annu. Rev. Biochem. 1999;68:729–777. - PubMed
    1. Cohen A.R., Woods D.F., Marfatia S.M., Walther Z., Chishti A.H., Anderson J.M., Wood D.F. Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells [published erratum appears in J. Cell Biol. 142:1157] J. Cell Biol. 1998;142:129–138. - PMC - PubMed
    1. Couchman J.R., Woods A. Syndecan-4 and integrinscombinatorial signaling in cell adhesion. J. Cell Sci. 1999;112:3415–3420. - PubMed
    1. Hsueh Y.P., Sheng M. Regulated expression and subcellular localization of syndecan heparan sulfate proteoglycans and the syndecan-binding protein CASK/LIN-2 during rat brain development. J. Neurosci. 1999;19:7415–7425. - PMC - PubMed