@article{Abdesselem2009Nogo6-7835,
  year={2009},
  doi={10.1523/JNEUROSCI.3561-09.2009},
  title={No Nogo66- and NgR-Mediated Inhibition of Regenerating Axons in the Zebrafish Optic Nerve},
  number={49},
  volume={29},
  issn={0270-6474},
  journal={The Journal of Neuroscience},
  pages={15489--15498},
  author={Abdesselem, Houari and Shypitsyna, Aleksandra and Solis Padilla, Gonzalo and Bodrikov, Vsevolod and Stürmer, Claudia}
}

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    <dcterms:title>No Nogo66- and NgR-Mediated Inhibition of Regenerating Axons in the Zebrafish Optic Nerve</dcterms:title>
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    <dc:creator>Stürmer, Claudia</dc:creator>
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    <dcterms:bibliographicCitation>First publ. in: The Journal of Neuroscience 29 (2009), 49, pp. 15489-15498</dcterms:bibliographicCitation>
    <dc:language>eng</dc:language>
    <dc:contributor>Solis Padilla, Gonzalo</dc:contributor>
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    <dc:contributor>Stürmer, Claudia</dc:contributor>
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    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:37:54Z</dc:date>
    <dc:contributor>Bodrikov, Vsevolod</dc:contributor>
    <dc:creator>Shypitsyna, Aleksandra</dc:creator>
    <dcterms:abstract xml:lang="eng">In contrast to mammals, lesioned axons in the zebrafish (ZF) optic nerve regenerate and restore vision. This correlates with the absence of the NogoA-specific N-terminal domains from the ZF nogo/rtn-4 (reticulon-4) gene that inhibits regeneration in mammals. However, mammalian nogo/rtn-4 carries a second inhibitory C-terminal domain, Nogo-66, being 70% identical with ZF-Nogo66. The present study examines, (1) whether ZF-Nogo66 is inhibitory and effecting similar signaling pathways upon Nogo66-binding to the Nogo66 receptor NgR and its coreceptors, and (2) whether Rat-Nogo66 on fish, and ZF-Nogo66 on mouse neurons, cause inhibition via NgR. Our results from "outgrowth, collapse and contact assays" suggest, surprisingly, that ZF-Nogo66 is growth-permissive for ZF and mouse neurons, quite in contrast to its Rat-Nogo66 homolog which inhibits growth. The opposite effects of ZF- and Rat-Nogo66 are, in both fish and mouse, transmitted by GPI (glycosylphosphatidylinositol)-anchored receptors, including NgR. The high degree of sequence homology in the predicted binding site is consistent with the ability of ZF- and mammalian-Nogo66 to bind to NgRs of both species. Yet, Rat-Nogo66 elicits phosphorylation of the downstream effector cofilin whereas ZF-Nogo66 has no influence on cofilin phosphorylation probably because of significantly different Rat- versus ZF-Nogo66 sequences outside of the receptor-binding region effecting, by speculation, recruitment of a different set of coreceptors or microdomain association of NgR. Thus, not only was the NogoA-specific domain lost in fish, but Nogo66, the second inhibitory domain in mammals, and its signaling upon binding to NgR, was modified so that ZF-Nogo/RTN-4 does not impair axon regeneration.</dcterms:abstract>
    <dc:contributor>Abdesselem, Houari</dc:contributor>
    <dc:creator>Bodrikov, Vsevolod</dc:creator>
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    <dc:creator>Solis Padilla, Gonzalo</dc:creator>
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    <dc:contributor>Shypitsyna, Aleksandra</dc:contributor>
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    <dc:creator>Abdesselem, Houari</dc:creator>
    <dcterms:issued>2009</dcterms:issued>
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