Please use this identifier to cite or link to this item: https://doi.org/10.1093/emboj/cdg570
Title: Nogo-A at CNS paranodes is a ligand of Caspr: Possible regulation of K + channel localization
Authors: Nie, 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.
Keywords: Caspr
K+ channel
Nogo-66 receptor
Nogo-A
Paranode
Issue Date: 3-Nov-2003
Citation: Nie, 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
Abstract: We 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.
Source Title: EMBO Journal
URI: http://scholarbank.nus.edu.sg/handle/10635/113567
ISSN: 02614189
DOI: 10.1093/emboj/cdg570
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