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Cntnap2  -  contactin associated protein-like 2

Mus musculus

Synonyms: 5430425M22Rik, Caspr2, Cell recognition molecule Caspr2, Contactin-associated protein-like 2, Kiaa0868, ...
 
 
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High impact information on Cntnap2

  • Furthermore, we show that the localization of Caspr2 and clustering of K+ channels at the juxtaparanodal region depends on the presence of TAG-1, an immunoglobulin-like cell adhesion molecule that binds Caspr2 [1].
  • In myelinated axons, K+ channels are concealed under the myelin sheath in the juxtaparanodal region, where they are associated with Caspr2, a member of the neurexin superfamily [1].
  • In the absence of TAG-1, axonal Caspr2 did not accumulate at juxtaparanodes, and the normal enrichment of shaker-type K+ channels in these regions was severely disrupted, in the central and peripheral nervous systems [2].
  • Kv1.1, Kv1.2, and Caspr2 all have PDZ binding sites and likely interact with the same PDZ binding protein [3].
  • In contrast, genetic disruption of the juxtaparanodal protein Caspr2 or the nodal cytoskeletal protein betaIV spectrin did not alter the paranodal cytoskeleton [4].
 

Anatomical context of Cntnap2

  • Here we investigated the distribution of Caspr2 during development of peripheral nerves of normal and galactolipids-deficient [ceramide galactosyl transferase (CGT)-/-] mice [5].
  • Caspr is present at the paranodal junction formed between the axon and myelinating glial cells, whereas Caspr2 is localized and associates with K(+) channels at the adjacent juxtaparanodal region [5].
  • In sciatic nerves of this mutant, Caspr2 was not found at the juxtaparanodal region but was concentrated instead at the paranodes with Kv1 [5].
 

Other interactions of Cntnap2

  • This transition was not observed in CGT mice, where Caspr2 and Kv1.2 remained paranodal [5].
  • Juxtaparanodal clustering of Shaker-like K+ channels in myelinated axons depends on Caspr2 and TAG-1 [1].
 

Analytical, diagnostic and therapeutic context of Cntnap2

  • Deletion of Caspr2 in mice by gene targeting revealed that it is required to maintain K+ channels at this location [1].

References

  1. Juxtaparanodal clustering of Shaker-like K+ channels in myelinated axons depends on Caspr2 and TAG-1. Poliak, S., Salomon, D., Elhanany, H., Sabanay, H., Kiernan, B., Pevny, L., Stewart, C.L., Xu, X., Chiu, S.Y., Shrager, P., Furley, A.J., Peles, E. J. Cell Biol. (2003) [Pubmed]
  2. Association of TAG-1 with Caspr2 is essential for the molecular organization of juxtaparanodal regions of myelinated fibers. Traka, M., Goutebroze, L., Denisenko, N., Bessa, M., Nifli, A., Havaki, S., Iwakura, Y., Fukamauchi, F., Watanabe, K., Soliven, B., Girault, J.A., Karagogeos, D. J. Cell Biol. (2003) [Pubmed]
  3. Recent progress on the molecular organization of myelinated axons. Scherer, S.S., Arroyo, E.J. J. Peripher. Nerv. Syst. (2002) [Pubmed]
  4. Spectrins and ankyrinB constitute a specialized paranodal cytoskeleton. Ogawa, Y., Schafer, D.P., Horresh, I., Bar, V., Hales, K., Yang, Y., Susuki, K., Peles, E., Stankewich, M.C., Rasband, M.N. J. Neurosci. (2006) [Pubmed]
  5. Localization of Caspr2 in myelinated nerves depends on axon-glia interactions and the generation of barriers along the axon. Poliak, S., Gollan, L., Salomon, D., Berglund, E.O., Ohara, R., Ranscht, B., Peles, E. J. Neurosci. (2001) [Pubmed]
 
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