A novel cytoplasmic domain of the p55 tumor necrosis factor receptor initiates the neutral sphingomyelinase pathway.

@article{Adam1996ANC,
  title={A novel cytoplasmic domain of the p55 tumor necrosis factor receptor initiates the neutral sphingomyelinase pathway.},
  author={Dieter Adam and Katja Wiegmann and Sabine Adam-Klages and Andrea J. Ruff and Martin Kroenke},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 24},
  pages={
          14617-22
        }
}
The human p55 tumor necrosis factor (TNF) receptor (TR55) initiates at least two independent signaling cascades. The acidic sphingomyelinase (A-SMase) pathway involves a phosphatidylcholine-specific phospholipase C, an endosomal A-SMase, and controls expression of multiple TNF-responsive genes through induction of transcription factors such as NF-kappaB. The neutral sphingomyelinase (N-SMase) pathway comprises a membrane-bound N-SMase, proline-directed protein kinases, as well as phospholipase… CONTINUE READING

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