p75 interacts with the Nogo receptor as a co-receptor for Nogo, MAG and OMgp

@article{Wang2002p75IW,
  title={p75 interacts with the Nogo receptor as a co-receptor for Nogo, MAG and OMgp},
  author={Kevin C. Wang and Jieun A. Kim and Rajeev Sivasankaran and Rosalind A. Segal and Zhigang He},
  journal={Nature},
  year={2002},
  volume={420},
  pages={74-78}
}
In inhibiting neurite outgrowth, several myelin components, including the extracellular domain of Nogo-A (Nogo-66), oligodendrocyte myelin glycoprotein (OMgp) and myelin-associated glycoprotein (MAG), exert their effects through the same Nogo receptor (NgR). The glycosyl phosphatidylinositol (GPI)-anchored nature of NgR indicates the requirement for additional transmembrane protein(s) to transduce the inhibitory signals into the interior of responding neurons. Here, we demonstrate that p75, a… 

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A Neutralizing Anti-Nogo66 Receptor Monoclonal Antibody Reverses Inhibition of Neurite Outgrowth by Central Nervous System Myelin*

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The p75 receptor acts as a displacement factor that releases Rho from Rho-GDI

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Molecular interactions of AMIGO family members in the Nogo receptor complex

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References

SHOWING 1-10 OF 28 REFERENCES

Myelin-Associated Glycoprotein as a Functional Ligand for the Nogo-66 Receptor

It is shown that MAG binds directly, with high affinity, to NgR, and Cleavage of GPI-linked proteins from axons protects growth cones from MAG-induced collapse, and dominant-negative NgR eliminates MAG inhibition of neurite outgrowth.

The p75 receptor transduces the signal from myelin-associated glycoprotein to Rho

It is shown that the neurotrophin receptor p75 (p75NTR) is the signal transducing element for myelin-associated glycoprotein (MAG), and Ganglioside GT1b, which is one of the binding partners of MAG, specifically associates with p75N TR, which may form a receptor complex for MAG to transmit the inhibitory signals in neurons.

Oligodendrocyte-myelin glycoprotein is a Nogo receptor ligand that inhibits neurite outgrowth

It is shown that a glycosylphosphatidylinositol-anchored CNS myelin protein, oligodendrocyte-myelin glycoprotein (OMgp), is a potent inhibitor of neurite outgrowth in cultured neurons and that Interfering with the OMgp/NgR pathway may allow lesioned axons to regenerate after injury in vivo.

Identification of a receptor mediating Nogo-66 inhibition of axonal regeneration

It is shown that the extracellular domain of Nogo (Nogo-66) inhibits axonal extension, but does not alter non-neuronal cell morphology, and a multivalent form of the N terminus of Noga-A affects the morphology of both neurons and other cell types.

Biochemical and functional interactions between the neurotrophin receptors trk and p75NTR

A close proximity of the two neurotrophin receptors within cell membranes is indicated, and it is suggested that the signalling pathways they initiate may interact soon after their activation.

Signalling through the neurotrophin receptor p75NTR

Bovine CNS Myelin Contains Neurite Growth-Inhibitory Activity Associated with Chondroitin Sulfate Proteoglycans

The results strongly suggest that brevican and versican V2 are additional components of CNS myelin that contribute to its nonpermissive substrate properties for axonal growth.