The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
Syndecan-4 Proteoglycan Regulates the Distribution and Activity of Protein Kinase C
Open accessAbstract
During cell-matrix adhesion, both tyrosine and serine/threonine kinases are activated. Integrin ligation correlates with tyrosine phosphorylation, whereas the later stages of spreading and focal adhesion and stress fiber formation in primary fibroblasts requires interactions of cell surface proteoglycan with heparin-binding moieties. This correlates with protein kinase C (PKC) activation, and PKCalpha can become localized to focal adhesions in normal, but not transformed, cells. PKC activation has been thought to be downstream of initial receptor-ligand interactions. We now show, however, that syndecan-4 transmembrane heparan sulfate proteoglycan and PKC co-immunoprecipitate and co-patch in vivo. The core protein of syndecan-4 can directly bind the catalytic domain of PKCalpha and potentiate its activation by phospholipid mediators. It can also directly activate PKCalpha in the absence of other mediators. This activity resides in the sequence LGKKPIYKK in the center of the short cytoplasmic domain, and other syndecans lack this sequence and PKC regulatory properties. Syndecan-4 is a focal adhesion component, and this interaction may both localize PKC and amplify its activity at sites of forming adhesions. This represents the first report of direct transmembrane signaling through cell surface proteoglycans.
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Cites
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Integrins and Signal Transduction Pathways: the Road Taken
Clark, E. A., & Brugge, J. S. (1995) · Science · doi:10.1126/science.7716514 · Cited by 2,937
FOCAL ADHESIONS, CONTRACTILITY, AND SIGNALING
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Integrin function: molecular hierarchies of cytoskeletal and signaling molecules.
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Biology of the Syndecans: A Family of Transmembrane Heparan Sulfate Proteoglycans
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Protein kinase C involvement in focal adhesion formation
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Cited by
Functions of Cell Surface Heparan Sulfate Proteoglycans
Bernfield, M., Götte, M., Park, P. W., Reizes, O., Fitzgerald, M. L., Lincecum, J., & Zako, M. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.729 · Cited by 2,688
Sarrazin, S., Lamanna, W. C., & Esko, J. D. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004952 · Cited by 1,516
Synergistic control of cell adhesion by integrins and syndecans
Morgan, M. R., Humphries, M. J., & Bass, M. D. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2289 · Cited by 583
The ins and outs of fibronectin matrix assembly
Wierzbicka-Patynowski, I., & Schwarzbauer, J. E. (2003) · Journal of Cell Science · doi:10.1242/jcs.00670 · Cited by 473
Saoncella, S., Echtermeyer, F., Denhez, F., Nowlen, J. K., Mosher, D. F., Robinson, S. D., Hynes, R. O., & Goetinck, P. F. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.2805 · Cited by 368
Metadata
- Authors
- Oh, E.-S., Woods, A., & Couchman, J. R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1997-03
- Volume
- 272
- Issue
- 13
- Pages
- 8133-8136
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1991708828
- Cited by
- 278
- References
- 19
- FWCI
- 10.27
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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