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The Journal of Neuroscience, June 1, 2005, 25(22):5298-5304; doi:10.1523/JNEUROSCI.5235-04.2005

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Development/Plasticity/Repair
Nogo-A Interacts with the Nogo-66 Receptor through Multiple Sites to Create an Isoform-Selective Subnanomolar Agonist

Fenghua Hu, Betty P. Liu, Stephane Budel, Ji Liao, Joanna Chin, Alyson Fournier, and Stephen M. Strittmatter

Departments of Neurology and Neurobiology, Yale University School of Medicine, New Haven, Connecticut 06520

Nogo is a myelin-derived protein that limits axonal regeneration after CNS injury. A short hydrophilic Nogo-66 loop between two hydrophobic domains of Nogo binds to a Nogo-66 receptor (NgR) to inhibit axonal outgrowth. Inhibition of axon outgrowth and cell spreading by a second Nogo domain, termed Amino-Nogo-A, is thought to be mediated by a distinct receptor complex. Here, we define a novel Nogo-A-specific domain in Amino-Nogo that binds to NgR with nanomolar affinity. This second domain of 24 amino acids does not alter cell spreading or axonal outgrowth. Fusion of the two NgR-binding Nogo-A domains creates a ligand with substantially enhanced affinity for NgR and converts a NgR antagonist peptide to an agonist. Thus, NgR activation by Nogo-A involves multiple sites of interaction between Nogo-A and NgR.

Key words: myelin; axon; regeneration; spinal cord injury; outgrowth inhibitor; cell spreading

Received Dec 22, 2004; revised April 17, 2005; accepted April 18, 2005.




This article has been cited by other articles:


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F. Hu and S. M. Strittmatter
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Characterization of Myelin Ligand Complexes with Neuronal Nogo-66 Receptor Family Members
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Subcutaneous Nogo Receptor Removes Brain Amyloid-{beta} and Improves Spatial Memory in Alzheimer's Transgenic Mice
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The Nogo-Nogo Receptor Pathway Limits a Spectrum of Adult CNS Axonal Growth.
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