The cytoplasmic domain of syndecan-1 is not required for association with Triton X-100-insoluble material.

@article{Miettinen1994TheCD,
  title={The cytoplasmic domain of syndecan-1 is not required for association with Triton X-100-insoluble material.},
  author={Heini M Miettinen and Markku Jalkanen},
  journal={Journal of cell science},
  year={1994},
  volume={107 ( Pt 6)},
  pages={1571-81}
}
Cell surface heparan sulfate proteoglycans such as syndecan-1 bind various extracellular matrix proteins and have been suggested to interact with the cytoskeleton. Such interactions are thought to be important for stabilizing cell morphology. Syndecan-1 resists extraction with Triton X-100. This insolubility was reported not to be affected by removal of the glycosaminoglycan chains, suggesting that the insolubility is not due to binding to the extracellular matrix, but rather to an association… CONTINUE READING