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- Title
Nogo-A at CNS paranodes is a ligand of Caspr: possible regulation of K<sup>+</sup> channel localization.
- Authors
Du-Yu Nie; Zhi-Hong Zhou; Beng-Ti Ang; Felicia Y.H. Teng; Gang Xu; Tao Xiang; Chao-yang Wang; Li Zeng; Yasuo Takeda; Tian-Le Xu; Yee-Kong Ng; Catherine Faivre-Sarrailh; Brian Popko; Eng-Ang Ling; Melitta Schachner; Kazutada Watanabe; Catherine J. Pallen; Bor Luen Tang; Zhi-Cheng Xiao
- 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.
- Publication
EMBO Journal, 2003, Vol 22, Issue 21, p5666
- ISSN
0261-4189
- Publication type
Academic Journal
- DOI
10.1093/emboj/cdg570