Please use this identifier to cite or link to this item: https://doi.org/10.1093/emboj/cdg570
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dc.titleNogo-A at CNS paranodes is a ligand of Caspr: Possible regulation of K + channel localization
dc.contributor.authorNie, D.-Y.
dc.contributor.authorZhou, Z.-H.
dc.contributor.authorAng, B.-T.
dc.contributor.authorTeng, F.Y.H.
dc.contributor.authorXu, G.
dc.contributor.authorXiang, T.
dc.contributor.authorWang, C.-Y.
dc.contributor.authorZeng, L.
dc.contributor.authorTakeda, Y.
dc.contributor.authorXu, T.-L.
dc.contributor.authorNg, Y.-K.
dc.contributor.authorFaivre-Sarrailh, C.
dc.contributor.authorPopko, B.
dc.contributor.authorLing, E.-A.
dc.contributor.authorSchachner, M.
dc.contributor.authorWatanabe, K.
dc.contributor.authorPallen, C.J.
dc.contributor.authorTang, B.L.
dc.contributor.authorXiao, Z.-C.
dc.date.accessioned2014-12-01T06:55:55Z
dc.date.available2014-12-01T06:55:55Z
dc.date.issued2003-11-03
dc.identifier.citationNie, D.-Y., Zhou, Z.-H., Ang, B.-T., Teng, F.Y.H., Xu, G., Xiang, T., Wang, C.-Y., Zeng, L., Takeda, Y., Xu, T.-L., Ng, Y.-K., Faivre-Sarrailh, C., Popko, B., Ling, E.-A., Schachner, M., Watanabe, K., Pallen, C.J., Tang, B.L., Xiao, Z.-C. (2003-11-03). Nogo-A at CNS paranodes is a ligand of Caspr: Possible regulation of K + channel localization. EMBO Journal 22 (21) : 5666-5678. ScholarBank@NUS Repository. https://doi.org/10.1093/emboj/cdg570
dc.identifier.issn02614189
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/113567
dc.description.abstractWe report Nogo-A as an oligodendroglial component congregating and interacting with the Caspr-F3 complex at paranodes. However, its receptor Nogo-66 receptor (NgR) does not segregate to specific axonal domains. CHO cells cotransfected with Caspr and F3, but not with F3 alone, bound specifically to substrates coated with Nogo-66 peptide and GST-Nogo-66. Binding persisted even after phosphatidylinositol-specific phospholipase C (PI-PLC) removal of GPI-linked F3 from the cell surface, suggesting a direct interaction between Nogo-66 and Caspr. Both Nogo-A and Caspr co-immunoprecipitated with Kv1.1 and Kv1.2, and the developmental expression pattern of both paralleled compared with Kv1.1, implicating a transient interaction between Nogo-A-Caspr and K + channels at early stages of myelination. In pathological models that display paranodal junctional defects (EAE rats, and Shiverer and CGT -/- mice), distances between the paired labeling of K+ channels were shortened significantly and their localization shifted toward paranodes, while paranodal Nogo-A congregation was markedly reduced. Our results demonstrate that Nogo-A interacts in trans with axonal Caspr at CNS paranodes, an interaction that may have a role in modulating axon-glial junction architecture and possibly K+-channel localization during development.
dc.sourceScopus
dc.subjectCaspr
dc.subjectK+ channel
dc.subjectNogo-66 receptor
dc.subjectNogo-A
dc.subjectParanode
dc.typeArticle
dc.contributor.departmentANATOMY
dc.contributor.departmentBIOCHEMISTRY
dc.description.doi10.1093/emboj/cdg570
dc.description.sourcetitleEMBO Journal
dc.description.volume22
dc.description.issue21
dc.description.page5666-5678
dc.description.codenEMJOD
dc.identifier.isiut000186448300002
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