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Gene Review

Cntnap1  -  contactin associated protein-like 1

Mus musculus

Synonyms: AI841080, Caspr, Caspr1, Contactin-associated protein 1, MHDNIV, ...
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Disease relevance of Cntnap1


High impact information on Cntnap1

  • This second type of translocation results in the transcription of a 7.0-kilobase chimaeric bcr/abl messenger RNA translated into a bcr/abl fusion protein, p190, which has an abnormal tyrosine kinase activity and is strongly autophosphorylated in vitro [4].
  • Transgenic expression of Nfasc155 in the myelinating glia of Nfasc-/- nerves rescues the axoglial adhesion complex by recruiting the axonal proteins Caspr and Contactin to the paranodes [5].
  • The mutation impedes intracellular transport and surface expression of Caspr and leaves NF155 on apposing paranodal myelin disengaged [6].
  • Loss of NCP1 also results in a severe decrease in peripheral nerve conduction velocity [2].
  • These structural changes were accompanied by a marked reduction of contactin-associated protein/paranodin, neurofascin 155 (NF155), and the potassium channel Kv1.2, whereas nodal clusters of sodium channels were unaltered [7].

Biological context of Cntnap1


Anatomical context of Cntnap1

  • 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 [11].
  • An axonal complex of cell adhesion molecules consisting of Caspr and contactin has been found to be essential for the generation of the paranodal axo-glial junctions flanking the nodes of Ranvier [8].
  • Clustering of contactin on the cell surface induced coclustering of Caspr and immobilized protein 4.1B at the plasma membrane [8].
  • Neurexin IV/Caspr1/paranodin (NCP1) is an important player in the formation of AGJs because it recruits a paranodal complex implicated in the tethering of glial proteins to the axonal membrane and cytoskeleton [12].
  • Furthermore, Caspr was distributed asymmetrically or was even absent in the mutant nerve fibers [13].

Associations of Cntnap1 with chemical compounds

  • Cell surface transport of F3/contactin and caspr/paranodin is insensitive to brefeldin A and the two glycoproteins are endoglycosidase H-sensitive when associated in complex, recruited into the lipid rafts, and expressed on the cell surface [1].
  • The presence of paranodin increased the association between integrin beta1 and schwannomin or its N-terminal domain, suggesting that the interactions between these proteins are interdependent [14].
  • Verification that the deduced primary structure was that of p190 was demonstrated through microsequence analysis of a cyanogen bromide peptide generated from chick brain p190 [15].

Physical interactions of Cntnap1

  • We show that the FERM domain of schwannomin binds to the paranodin GNP motif in glutathione S-transferase (GST)-pull down assays and in transfected COS-7 cells [14].
  • These results suggest that Caspr serves as a "transmembrane scaffold" that stabilizes the Caspr/contactin adhesion complex at the paranodal junction by connecting it to cytoskeletal components within the axon [8].
  • The formation of these specialized axoglial contacts depends on the presence of three cell adhesion molecules: neurofascin 155 on the glial membrane and a complex of Caspr and contactin on the axon [16].

Other interactions of Cntnap1


Analytical, diagnostic and therapeutic context of Cntnap1

  • Using immunoelectron microscopy, we found that a Caspr mutant lacking its intracellular domain was often found within the axon instead of the junctional axolemma [8].
  • In contrast to the PNS, K(+) channels were initially expressed fully segregated from nodes and paranodes, the latter identified by immunofluorescence of Caspr, a component of axoglial junctions [19].


  1. The paranodal complex of F3/contactin and caspr/paranodin traffics to the cell surface via a non-conventional pathway. Bonnon, C., Goutebroze, L., Denisenko-Nehrbass, N., Girault, J.A., Faivre-Sarrailh, C. J. Biol. Chem. (2003) [Pubmed]
  2. Axon-glia interactions and the domain organization of myelinated axons requires neurexin IV/Caspr/Paranodin. Bhat, M.A., Rios, J.C., Lu, Y., Garcia-Fresco, G.P., Ching, W., St Martin, M., Li, J., Einheber, S., Chesler, M., Rosenbluth, J., Salzer, J.L., Bellen, H.J. Neuron (2001) [Pubmed]
  3. Antigen-induced B lymphocyte activation involves the p21ras and ras.GAP signaling pathway. Lazarus, A.H., Kawauchi, K., Rapoport, M.J., Delovitch, T.L. J. Exp. Med. (1993) [Pubmed]
  4. Acute leukaemia in bcr/abl transgenic mice. Heisterkamp, N., Jenster, G., ten Hoeve, J., Zovich, D., Pattengale, P.K., Groffen, J. Nature (1990) [Pubmed]
  5. Neurofascins are required to establish axonal domains for saltatory conduction. Sherman, D.L., Tait, S., Melrose, S., Johnson, R., Zonta, B., Court, F.A., Macklin, W.B., Meek, S., Smith, A.J., Cottrell, D.F., Brophy, P.J. Neuron (2005) [Pubmed]
  6. Contactin orchestrates assembly of the septate-like junctions at the paranode in myelinated peripheral nerve. Boyle, M.E., Berglund, E.O., Murai, K.K., Weber, L., Peles, E., Ranscht, B. Neuron (2001) [Pubmed]
  7. The raft-associated protein MAL is required for maintenance of proper axon--glia interactions in the central nervous system. Schaeren-Wiemers, N., Bonnet, A., Erb, M., Erne, B., Bartsch, U., Kern, F., Mantei, N., Sherman, D., Suter, U. J. Cell Biol. (2004) [Pubmed]
  8. Retention of a cell adhesion complex at the paranodal junction requires the cytoplasmic region of Caspr. Gollan, L., Sabanay, H., Poliak, S., Berglund, E.O., Ranscht, B., Peles, E. J. Cell Biol. (2002) [Pubmed]
  9. Dependence of nodal sodium channel clustering on paranodal axoglial contact in the developing CNS. Rasband, M.N., Peles, E., Trimmer, J.S., Levinson, S.R., Lux, S.E., Shrager, P. J. Neurosci. (1999) [Pubmed]
  10. Mice lacking sodium channel beta1 subunits display defects in neuronal excitability, sodium channel expression, and nodal architecture. Chen, C., Westenbroek, R.E., Xu, X., Edwards, C.A., Sorenson, D.R., Chen, Y., McEwen, D.P., O'Malley, H.A., Bharucha, V., Meadows, L.S., Knudsen, G.A., Vilaythong, A., Noebels, J.L., Saunders, T.L., Scheuer, T., Shrager, P., Catterall, W.A., Isom, L.L. J. Neurosci. (2004) [Pubmed]
  11. 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]
  12. Disruption of axo-glial junctions causes cytoskeletal disorganization and degeneration of Purkinje neuron axons. Garcia-Fresco, G.P., Sousa, A.D., Pillai, A.M., Moy, S.S., Crawley, J.N., Tessarollo, L., Dupree, J.L., Bhat, M.A. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  13. Altered expression of ion channel isoforms at the node of Ranvier in P0-deficient myelin mutants. Ulzheimer, J.C., Peles, E., Levinson, S.R., Martini, R. Mol. Cell. Neurosci. (2004) [Pubmed]
  14. Association of Caspr/paranodin with tumour suppressor schwannomin/merlin and beta1 integrin in the central nervous system. Denisenko-Nehrbass, N., Goutebroze, L., Galvez, T., Bonnon, C., Stankoff, B., Ezan, P., Giovannini, M., Faivre-Sarrailh, C., Girault, J.A. J. Neurochem. (2003) [Pubmed]
  15. Primary structure and cellular localization of chicken brain myosin-V (p190), an unconventional myosin with calmodulin light chains. Espreafico, E.M., Cheney, R.E., Matteoli, M., Nascimento, A.A., De Camilli, P.V., Larson, R.E., Mooseker, M.S. J. Cell Biol. (1992) [Pubmed]
  16. 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]
  17. Contactin supports synaptic plasticity associated with hippocampal long-term depression but not potentiation. Murai, K.K., Misner, D., Ranscht, B. Curr. Biol. (2002) [Pubmed]
  18. Myelinating Schwann cells determine the internodal localization of Kv1.1, Kv1.2, Kvbeta2, and Caspr. Arroyo, E.J., Xu, Y.T., Zhou, L., Messing, A., Peles, E., Chiu, S.Y., Scherer, S.S. J. Neurocytol. (1999) [Pubmed]
  19. K+ channel distribution and clustering in developing and hypomyelinated axons of the optic nerve. Rasband, M.N., Trimmer, J.S., Peles, E., Levinson, S.R., Shrager, P. J. Neurocytol. (1999) [Pubmed]
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