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Identification of a novel contactin‐associated transmembrane receptor with multiple domains implicated in protein–protein interactions
Open accessAbstract
Receptor protein tyrosine phosphatase beta (RPTPbeta) expressed on the surface of glial cells binds to the glycosylphosphatidylinositol (GPI)-anchored recognition molecule contactin on neuronal cells leading to neurite outgrowth. We describe the cloning of a novel contactin-associated transmembrane receptor (p190/Caspr) containing a mosaic of domains implicated in protein-protein interactions. The extracellular domain of Caspr contains a neurophilin/coagulation factor homology domain, a region related to fibrinogen beta/gamma, epidermal growth factor-like repeats, neurexin motifs as well as unique PGY repeats found in a molluscan adhesive protein. The cytoplasmic domain of Caspr contains a proline-rich sequence capable of binding to a subclass of SH3 domains of signaling molecules. Caspr and contactin exist as a complex in rat brain and are bound to each other by means of lateral (cis) interactions in the plasma membrane. We propose that Caspr may function as a signaling component of contactin, enabling recruitment and activation of intracellular signaling pathways in neurons. The binding of RPTPbeta to the contactin-Caspr complex could provide a mechanism for cell-cell communication between glial cells and neurons during development.
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“In comparison to Caspr, which becomes concentrated in the paranodal junctions of myelinated axons [49], BIN1 displayed patchy distribution along short segments of interdigitating processes without an apparent concentration in the nodes or the paranodal area (Fig. 4g).”
From Predominant expression of Alzheimer’s disease-associated BIN1 in mature oligodendrocytes and localization to white matter tracts (2016) · cites this paper as [49]
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“…of how these et al., 1999; 1:500–1:1000) mouse monoclonal and rabbit polyclonal glycolipids affect the formation of paranodal junctions antibodies to Caspr-1 (Peles et al., 1997; 1:200 and 1:2000); rabbit anti-NF155 (Tait et al., 2000; 1:100); mouse monoclonal anti-ankyrinremains less clear.”
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“This peptide does have partial homology (6 of 7 amino acids, V /L RPMPLQ ) to the laminin-G domain of contactin-associated protein 1 (Caspr-1), which is present in human intestine and might be involved in contactin-mediated cell signaling and in tumor metastasis and invasio”
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“To test this, we immunostained ventral roots at the acute progressive phase with an antibody to Caspr, a cell adhesion molecule at the paranodal axolemma that is essential for the formation of the axoglial junctions (Einheber et al., 1997; Menegoz et al., 1997; Peles et al., 1997; Bhat et al., 2001; Rios et al., 2003)…”
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“Blots were prehybridized, hybridized, and washed using standard techniques; the final stringency of the wash was 0.2 3 SSC at 65 8 C for 30 min. cDNAs used as probes included an z 500-bp fragment to rat Caspr and an z 1.5-kb fragment to human contactin as described (Peles et al., 1997 b ).”
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“The axo-glial adhesion zone and the invertebrate septate junction both contain members of the NCP (for neurexin IV, Caspr1/paranodin, and Caspr2) subgroup of the neurexin superfamily (Menegoz et al., 1997; Peles et al., 1997a, b; Bellen et al., 1998; Po-”
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“The polyclonal anti-Caspr was generated against a bacterial fusion protein containing the cytoplasmic domain and was used at a dilution of 1:2500 (Peles et al., 1997).”
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“antibodies to Caspr (Peles et al., 1997; Poliak et al., 1999), chick anti-βIV spectrin (Komada and Soriano, 2002), and rabbit anti-”
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“…and to paranodin/caspr, a protein crucial for formation of the para-by blocking its ability to bind to b2. nodal axon-glial junction (Isom et al., 1995; Peles et al., 1997; Faivre-Sarrailh et al., 2000; Isom, 2000; Rios et al.,How Are Nodal and Internodal Domains Specified and Maintained?”
BackgroundRios, J. C., Melendez-Vasquez, C., Einheber, S., Lustig, M., Grumet, M., Hemperly, J., Peles, E., & Salzer, J. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-22-08354.2000 · Cited by 287
“In previous studies we presented evidence that Caspr and contactin interact laterally in the membrane (Peles et al., 1997) but were able to detect only Caspr in the paranodal junctions (Einheber et al., 1997).”
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“forming a trimeric complex between neurexin, contactin, and RPTPb at the junction of neurons with glial cells (29).”
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“other transmembrane proteins, in either the same or adjoining cells (Peles et al., 1997).”
BackgroundAxo-Glial Interactions Regulate the Localization of Axonal Paranodal Proteins
Dupree, J., Girault, J., & Popko, B. (1999) · Journal of Cell Biology · doi:10.1083/jcb.147.6.1145 · Cited by 278
“This protein was also identified as a partner of contactin, a glycosyl-phosphatidyl-inositol–anchored adhesion molecule, and termed contactin-associated protein (Caspr) (Peles et al., 1997).”
BackgroundNeurofascin as a target for autoantibodies in peripheral neuropathies
Ng, J., Malotka, J., Kawakami, N., Derfuss, T., Khademi, M., Olsson, T., Linington, C., Odaka, M., Tackenberg, B., Prüss, H., et al. (2012) · Neurology · doi:10.1212/wnl.0b013e31827689ad · Cited by 270
Self-citationBlack, J., Nikolajsen, L., Krøner, K., Jensen, T. S., & Waxman, S. G. (2008) · Annals of Neurology · doi:10.1002/ana.21527 · Cited by 270
“6 is the predominant sodium channel at nodes of Ranvier where it is expressed at a high density(41) and Caspr demarcates paranodal regions.(42) Samples that did not exhibit Nav1.”
BackgroundParanodin, a Glycoprotein of Neuronal Paranodal Membranes
Menegoz, M., Gaspar, P., Bert, M. L., Galvez, T., Burgaya, F., Palfrey, C., Ezan, P., Arnos, F., & Girault, J. (1997) · Neuron · doi:10.1016/s0896-6273(00)80942-3 · Cited by 256
Ishibashi, T., Dupree, J., Ikenaka, K., Hirahara, Y., Honke, K., Peles, E., Popko, B., Suzuki, K., Nishino, H., & Baba, H. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-15-06507.2002 · Cited by 248
“In addition, contactin-associated protein (Caspr) and its binding partner, contactin, form a complex at the paranodal junctions (Peles et al., 1997; Faivre-Sarrailh et al., 2000; Rios et al., 2000) and may physically separate these two channels by inhibiting lateral movement of these proteins.”
BackgroundMethodSelf-citationMolecular domains of myelinated axons.
Peles, E., & Salzer, J. (2000) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(00)00122-7 · Cited by 242
“The extracellular region of Caspr is a mosaic of domains implicated in mediating protein–protein and protein–carbohydrate interactions, including discoidinand fibrinogen-like domains, EGF motifs and LNS domains [11,42].”
BackgroundInfluentialSelf-citationThe Classical Arabinogalactan Protein Gene Family of Arabidopsis
Schultz, C., Johnson, K. L., Currie, G., & Bacic, A. (2000) · The Plant Cell · doi:10.1105/tpc.12.9.1751 · Cited by 242
“These interactions can be with proteins in the same cell as the GPIanchored protein or in neighboring cells (Peles et al., 1997).”
BackgroundMolecular domains of myelinated axons in the peripheral nervous system
Salzer, J. L., Brophy, P., & Peles, E. (2008) · Glia · doi:10.1002/glia.20750 · Cited by 230
“…contactin form a tight cis complex required for the expression of Caspr at the cell surface and for the localization of contactin at the paranode (Bhat et al., 2001; Bonnon et al., 2007; Boyle et al., 2001; FaivreSarrailh et al., 2000; Gollan et al., 2003; Peles et al., 1997; Rios et al., 2000).”
BackgroundSelf-citationVerkerk, A., Mathews, C., Joosse, M., Eussen, B., Heutink, P., & Oostra, B. (2003) · Genomics · doi:10.1016/s0888-7543(03)00097-1 · Cited by 237
“CNTNAP2 and CNTNAP1, another member of this family, are localized to the axonal nodes of Ranvier, but to different, distinct, compartments [24,31,33,34].”
BackgroundNguyen, T., & Südhof, T. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.41.26032 · Cited by 234
Krämer, E., Klein, C., Koch, T., Boytinck, M., & Trotter, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.41.29042 · Cited by 232
Anderson, G. R., Galfin, T., Xu, W., Aoto, J. N., Malenka, R. C., & Südhof, T. C. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1216398109 · Cited by 234
“Moreover, in Drosophila the CASPR2 homolog neurexin IV binds not only to contactins similar to its vertebrate counterpart (33) but also to other Ig-domain proteins such as neurofascin, wrapper, and roundabout (40–42).”
BackgroundAtaxia and abnormal cerebellar microorganization in mice with ablated contactin gene expression.
Berglund, E., Murai, K., Fredette, B., Sekerkovâ, G., Marturano, B., Weber, L., Mugnaini, E., & Ranscht, B. (1999) · Neuron · doi:10.1016/s0896-6273(00)81126-5 · Cited by 216
alpha-Latrotoxin and its receptors: neurexins and CIRL/latrophilins.
Südhof, T. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.933 · Cited by 215
“…because its naming erroneously suggests that it belongs to the same family as vertebrate neurexins, whereas in fact it is the Drosophila homolog of vertebrate CASPR/paranodin proteins that exhibit a distant resemblance to neurexins (Peles et al 1997a,b; Menegoz et al 1997; Poliak et al 1999).”
BackgroundPillai, A. M., Thaxton, C., Pribisko, A. L., Cheng, J., Dupree, J. L., & Bhat, M. A. (2009) · Journal of Neuroscience Research · doi:10.1002/jnr.22015 · Cited by 202
“Three major paranodal proteins have been identified: Caspr or paranodin (Einheber et al., 1997; Menegoz et al., 1997; Peles et al., 1997; Bhat et al., 2001), and a GPI-anchored neural cell adhesion molecule Contactin (Cont; Berglund et al., 1999; Boyle et al., 2001) on the axonal side, and…”
Miura, Y., Devaux, J., Fukami, Y., Manso, C., Belghazi, M., Wong, A. H. Y., & Yuki, N. (2015) · Brain : a journal of neurology · doi:10.1093/brain/awv054 · Cited by 212
“CNTN1 is a key axonal adhesion molecule, which interacts with CNTNAP1 (previously known as Caspr1) on the axon and neurofascin-155 on the glial side (Peles et al., 1997; Tait et al., 2000), and is essential for the formation of the paranodal septate-like junction (Boyle et al., 2001).”
BackgroundSusuki, K., Baba, H., Tohyama, K., Kanai, K., Kuwabara, S., Hirata, K., Furukawa, K., Furukawa, K., Rasband, M. N., & Yuki, N. (2007) · Glia · doi:10.1002/glia.20503 · Cited by 197
“The polyclonal and monoclonal anti-Caspr antibodies were kind gifts from Dr. E. Peles (Weizmann Institute of Science, Rehovot, Israel) (Peles et al., 1997).”
MethodFeinberg, K., Eshed‐Eisenbach, Y., Frechter, S., Amor, V., Salomon, D., Sabanay, H., Dupree, J. L., Grumet, M., Brophy, P., Shrager, P. G., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.02.004 · Cited by 210
“Rabbit polyclonal antibodies against gliomedin (Eshed et al., 2007), Caspr (Peles et al., 1997), NrCAM (Lustig et al., 2001), mouse monoclonal antibodies against gliomedin (Eshed et al., 2005), and Caspr (Poliak et al., 1999) were all described.”
BackgroundSelf-citationChen, C.-L., Bharucha, V., Chen, Y., Westenbroek, R., Brown, A. M., Malhotra, J., Jones, D. M., Avery, C., Gillespie, P., Kazen-Gillespie, K., et al. (2002) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.212638099 · Cited by 203
GPI-anchors on arabinogalactan-proteins: implications for signalling in plants
Schultz, C., Gilson, P., Oxley, D., Youl, J., & Bacic, A. (1998) · doi:10.1016/s1360-1385(98)01328-4 · Cited by 200
Doppler, K., Appeltshauser, L., Villmann, C., Martin, C., Peles, E., Krämer, H., Haarmann, A., Buttmann, M., & Sommer, C. (2016) · Brain : a journal of neurology · doi:10.1093/brain/aww189 · Cited by 199
“…poly-D-lysine-coated cover slips in a 24-well-plate at a density of 50 000 cells/well and were transiently transfected with plasmids of human Caspr (Peles et al., 1997) or human contactin-1 as a control (Peles et al., 1995) using the calcium-phosphate precipitation method (0.25 mg of DNA/well) as…”
InfluentialSelf-citationContactin Associates with Na+ Channels and Increases Their Functional Expression
Kazarinova-Noyes, K., Malhotra, J., Mcewen, D. P., Mattei, L. N., Berglund, E., Ranscht, B., Levinson, S., Schachner, M., Shrager, P., Isom, L., et al. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-19-07517.2001 · Cited by 199
“…(Caspr)/paranodin, a neurexin family protein that forms part of the axoglial junctions at paranodes (Einheber et al., 1997; Menegoz et al., 1997; Peles et al., 1997; Faivre-Sarrailh et al., 2000; Rios et al., 2000) and whose expression precedes Na channel clustering in the optic nerve (Rasband…”
BackgroundMcGonigal, R., Rowan, E., Greenshields, K., Halstead, S., Humphreys, P., Rother, R., Furukawa, K., & Willison, H. (2010) · Brain : a journal of neurology · doi:10.1093/brain/awq119 · Cited by 198
“At the paranode, the axo-glial junction is formed by the axolemmal proteins contactin and Caspr, while neurofascin 155 is the glial receptor to this complex (Charles et al., 2002;Einheber et al., 1997;Menegoz et al., 1997;Peles et al., 1997;Rios et al., 2000;Tait et al., 2000).”
BackgroundMechanisms and Roles of Axon-Schwann Cell Interactions
Corfas, G., Velardez, M., Ko, C.-P., Ratner, N., & Peles, E. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.3649-04.2004 · Cited by 197
“The axonal membrane at the paranodes contains a complex of cell adhesion molecules that include Caspr (Einheber et al., 1997; Peles et al., 1997) [contactin-associated protein, also known as paranodin (Menegoz et al.”
BackgroundInfluentialSelf-citationWhite, R., Gonsior, C., Krämer-Albers, E.-M., Stöhr, N., Hüttelmaier, S., & Trotter, J. (2008) · Journal of Cell Biology · doi:10.1083/jcb.200706164 · Cited by 194
“The cis association of F3 in oligodendrocytes with another transmembrane molecule such as Caspr or protein tyrosine phosphatase , as shown in neurons, may aid in F3-mediated signal transduction ( Peles et al., 1997 ; Zeng et al., 1999 ).”
BackgroundIwamoto, K., Bundo, M., Ueda, J., Oldham, M. C., Ukai, W., Hashimoto, E., Saito, T., Geschwind, D. H., & Kato, T. (2011) · Genome Research · doi:10.1101/gr.112755.110 · Cited by 189
“CNTNAP1 encodes an axonal protein important for cell–cell communication between neurons and glias (Peles et al. 1997).”
BackgroundZonta, B., Tait, S., Melrose, S., Anderson, H., Harroch, S., Higginson, J., Sherman, D. L., & Brophy, P. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200712154 · Cited by 188
“…between the glial isoform of Neurofascin, Nfasc155, and the axonal proteins Caspr (also known as Paranodin) and Contactin ( Menegoz et al., 1997 ; Peles et al., 1997 ; Tait et al., 2000 ; Bhat et al., 2001 ; Boyle et al., 2001 ; Kazarinova-Noyes et al., 2001 ; Charles et al., 2002 ; Sherman and…”
BackgroundHuai, J., & Drescher, U. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008127200 · Cited by 185
Rios, J. C., Rubin, M. B., Martin, M. S. S., Downey, R., Einheber, S., Rosenbluth, J., Levinson, S. R., Bhat, M., & Salzer, J. L. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-18-07001.2003 · Cited by 178
“The adhesion molecules contactin and Caspr (contactinassociated protein) form a cis complex on axons that is concentrated at the junctions (Einheber et al., 1997; Menegoz et al., 1997; Peles et al., 1997; Rios et al., 2000).”
BackgroundHossain, W. A., Antic, S. D., Yang, Y., Rasband, M. N., & Morest, D. K. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0123-05.2005 · Cited by 181
“Mouse monoclonal (Rasband and Trimmer, 2001) and rabbit polyclonal anti-Caspr antibodies were made against the same fusion protein as for previously characterized anti-Caspr polyclonal rabbit antibodies (Peles et al., 1997).”
BackgroundThe node of Ranvier in CNS pathology
Arancibia-Carcamo, I. L., & Attwell, D. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1305-z · Cited by 177
Sakurai, T., Lustig, M., Nativ, M., Hemperly, J., Schlessinger, J., Peles, E., & Grumet, M. (1997) · Journal of Cell Biology · doi:10.1083/jcb.136.4.907 · Cited by 176
“Alternatively, a recently identified contactinassociated transmembrane protein of 190 kD that coprecipitates with RPTPb (Peles et al., 1995, 1997) may be involved in transducing neurite growth signals generated by RPTPb. Nr-CAM might also act in signaling by linking to the cytoskeleton via ankyrin…”
BackgroundSelf-citationGarwood, J., Schnädelbach, O., Clement, A. M., Schütte, K., Bach, A., & Faissner, A. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-10-03888.1999 · Cited by 168
“Bacterially and eukaryotically expressed protein domain constructs corresponding to different parts of the core protein of phosphacan/RPTPb/z have been tested in neurite outgrowth assays (Peles et al., 1995, 1997; Sakurai et al., 1997).”
MethodThe tenascin gene family in axon growth and guidance
Faissner, A. (1997) · Cell and Tissue Research · doi:10.1007/s004410050938 · Cited by 170
“This Ig superfamily member thus appears as a versatile integrator of neural ECM influences on neuronal differentiation, influences that might impinge on signal transduction pathways via the associated transducer CAPSR and the non-receptor tyrosine kinase fyn (Cervello et al. 1996; Peles et al. 1997).”
BackgroundOxley, D., & Bacic, A. (1999) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.96.25.14246 · Cited by 169
Faivre-Sarrailh, C., Banerjee, S., Li, J., Hortsch, M., Laval, M., & Bhat, M. (2004) · Development · doi:10.1242/dev.01372 · Cited by 168
“The physiological interaction between vertebrate NCP1 and contactin suggested that a similar molecular complex might exist at the invertebrate SJs.”
BackgroundInfluentialNew insights into the metabolic and molecular basis for diabetic neuropathy
Sima, A. A. F. (2003) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-003-3084-x · Cited by 155
The genetics of the protein 4.1 family: organizers of the membrane and cytoskeleton.
Hoover, K. B., & Bryant, P. (2000) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(99)00080-0 · Cited by 163
Missler, M., Fernández-Chacón, R., & Südhof, T. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.71041339.x · Cited by 161
Developmental clustering of ion channels at and near the node of Ranvier.
Rasband, M., & Trimmer, J. S. (2001) · Developmental Biology · doi:10.1006/dbio.2001.0326 · Cited by 158
Contactin-1 IgG4 antibodies cause paranode dismantling and conduction defects.
Manso, C., Querol, L., Mekaouche, M., Illa, I., & Devaux, J. (2016) · Brain : a journal of neurology · doi:10.1093/brain/aww062 · Cited by 155
“CNTN1 and its partner contactin-associated protein-1 (CASPR1, encoded by CNTNAP1) are expressed on the axonal surface and interact with NF155 located on the closely apposed glial loops (Peles et al., 1997; Rios et al., 2000; Charles et al., 2002).”
Caspr regulates the processing of contactin and inhibits its binding to neurofascin
Gollan, L., Salomon, D., Salzer, J., & Peles, E. (2003) · Journal of Cell Biology · doi:10.1083/jcb.200309147 · Cited by 154
“The lack of Caspr-Fc binding to the latter was expected because these molecules only interact when both are present on the same membrane (i.e., in cis; Peles et al., 1997).”
Self-citationYang, Y., Lacas-Gervais, S., Morest, D., Solimena, M., & Rasband, M. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.2125-04.2004 · Cited by 153
“In contrast, the amount of Caspr (a paranodal protein) (Peles et al., 1997) was reduced in qv3J animals compared with WT, but the levels of Kv1.”
ResultPoliak, S., Gollan, L., Salomon, D., Berglund, E., Ohara, R., Ranscht, B., & Peles, E. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-19-07568.2001 · Cited by 153
Self-citationDe Rossi, P., Buggia-Prévot, V., Clayton, B. L. L., Vasquez, J. B., van Sanford, C., Andrew, R. J., Lesnick, R., Botté, A., Deyts, C., Salem, S., et al. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0124-1 · Cited by 151
“In comparison to Caspr, which becomes concentrated in the paranodal junctions of myelinated axons [49], BIN1 displayed patchy distribution along short segments of interdigitating processes without an apparent concentration in the nodes or the paranodal area (Fig.”
Contactins: Emerging key roles in the development and function of the nervous system
Shimoda, Y., & Watanabe, K. (2009) · Cell Adhesion & Migration · doi:10.4161/cam.3.1.7764 · Cited by 149
Does Paranode Formation and Maintenance Require Partitioning of Neurofascin 155 into Lipid Rafts?
Schafer, D. P., Bansal, R., Hedstrom, K. L., Pfeiffer, S., & Rasband, M. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.5427-03.2004 · Cited by 146
“Polyclonal (affinity purified) and monoclonal (IgM) anti-Caspr antibodies were made against a Caspr-fusion protein kindly provided by Dr. Elior Peles (The Weizman Institute of Science, Rehovot, Israel) ( Peles et al., 1997 ).”
MethodDenisenko‐Nehrbass, N., Oguievetskaia, K., Goutebroze, L., Galvez, T., Yamakawa, H., Ohara, O., Carnaud, M., & Girault, J. (2003) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2003.02441.x · Cited by 142
“…a transmembrane glycoprotein associated with contactin (or F3), is highly enriched in the axolemma of paranodal septatelike junctions, on either sides of nodes of Ranvier in the myelinated fibers of the central and peripheral nervous systems (Menegoz et al., 1997; Peles et al., 1997).”
BackgroundSodium channel Na(v)1.6 is expressed along nonmyelinated axons and it contributes to conduction.
Black, J., Renganathan, M., & Waxman, S. (2002) · Brain Research. Molecular Brain Research · doi:10.1016/s0169-328x(02)00385-6 · Cited by 142
Ojeda, S., Lomniczi, A., & Sandau, U. (2008) · Journal of neuroendocrinology · doi:10.1111/j.1365-2826.2008.01712.x · Cited by 139
F3/contactin, a neuronal cell adhesion molecule implicated in axogenesis and myelination
Falk, J., Bonnon, C., Girault, J., & Faivre-Sarrailh, C. (2002) · Biology of the Cell · doi:10.1016/s0248-4900(02)00006-0 · Cited by 139
“Caspr/Paranodin binds laterally F3/contactin when both proteins are expressed in the same cell (i.e., cis interactions; Peles et al., 1997).”
BackgroundMyelin-associated glycoprotein and myelin galactolipids stabilize developing axo-glial interactions
Marcus, J., Dupree, J., & Popko, B. (2002) · Journal of Cell Biology · doi:10.1083/jcb.200111047 · Cited by 138
“…[Upstate Biotechnology]; Caspr/paranodin (rabbit polyclonal, a gift from Dr. Elior Peles, The Weizmann Institute of Science, Rehovot, Israel [Peles et al., 1997]); neurofascin 155 (rabbit polyclonal, gift from Dr. Peter Brophy, University of Edinburgh, Edinburgh, UK [Tait et al., 2000]);…”
BackgroundMechanisms of node of Ranvier assembly
Rasband, M. N., & Peles, E. (2020) · Nature reviews. Neuroscience · doi:10.1038/s41583-020-00406-8 · Cited by 180
Self-citationBellen, H. J., Lu, Y.-L., Beckstead, R. B., & Bhat, M. (1998) · Trends in Neurosciences · doi:10.1016/s0166-2236(98)01267-3 · Cited by 137
The role of sodium channels in cell adhesion
Lori, L. I. (2002) · Frontiers in bioscience · doi:10.2741/isom · Cited by 125
“Contactin is linked to the localization of axonal ion channels through its association with Caspr/paranodin, a neurexin-family protein that forms part of the axoglial junctions at paranodes (73-77), and whose expression precedes sodium channel clustering in the optic nerve (78).”
BackgroundGalactolipids are molecular determinants of myelin development and axo-glial organization.
Marcus, J., & Popko, B. (2002) · Biochimica et Biophysica Acta · doi:10.1016/s0304-4165(02)00410-5 · Cited by 131
Wang, X., Roy, P. J., Holland, S., Zhang, L.-J. W., Culotti, J., & Pawson, T. (1999) · Molecules and Cells · doi:10.1016/s1097-2765(00)80220-8 · Cited by 130
Wolswijk, G., & Balesar, R. (2003) · Brain : a journal of neurology · doi:10.1093/brain/awg151 · Cited by 129
“…axons in the CNS and PNS and that has been implicated in the formation and maintenance of the paranodal junctions is the Drosophila Neurexin IV-related molecule contactin-associated protein (Caspr), also termed paranodin (Einheber et al., 1997; Menegoz et al., 1997; Peles et al., 1997a,b).”
BackgroundInfluentialMechanisms of sodium channel clustering and its influence on axonal impulse conduction
Freeman, S. A., Desmazières, A., Fricker, D., Lubetzki, C., & Sol‐Foulon, N. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2081-1 · Cited by 149
Faivre-Sarrailh, C., Gauthier, F., Denisenko‐Nehrbass, N., Bivic, A. L., Rougon, G., & Girault, J. (2000) · Journal of Cell Biology · doi:10.1083/jcb.149.2.491 · Cited by 124
“The results of the present study suggest that the lack of association with Fyn of the truncated F3-Ig form, could be secondary to its lack of sorting into microdomains.”
BackgroundInfluentialMyelinating Schwann cells determine the internodal localization of Kv1.1, Kv1.2, Kvβ2, and Caspr
Arroyo, E., Xu, Y.-T., Zhou, L., Messing, A., Peles, E., Chiu, S. Y., & Scherer, S. (1999) · Journal of Neurocytology · doi:10.1023/a:1007009613484 · Cited by 124
“The paranodal axonal membrane contains contactin-associated protein (Caspr) (Einheber et al., 1997; Peles et al., 1997), also known as paranodin (Menegoz et al., 1997), a putative cell adhesion molecule that may link the axonal and glial membranes.”
BackgroundSelf-citationVural, A., Doppler, K., & Meinl, E. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01029 · Cited by 134
Proteomic analysis of synaptosomes using isotope‐coded affinity tags and mass spectrometry
Schrimpf, S., Meskenaïte, V., Brunner, E., Rutishauser, D., Walther, P., Eng, J. K., Aebersold, R. H., & Sonderegger, P. (2005) · PROTEOMICS · doi:10.1002/pmic.200401198 · Cited by 125
Mcewen, D. P., & Isom, L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405990200 · Cited by 121
Funatsu, N., Miyata, S., Kumanogoh, H., Shigeta, M., Hamada, K., Endo, Y., Sokawa, Y., & Maékawa, S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.12.8224 · Cited by 119
Autoimmune antigenic targets at the node of Ranvier in demyelinating disorders
Stathopoulos, P., Alexopoulos, H., & Dalakas, M. C. (2015) · Nature Reviews Neurology · doi:10.1038/nrneurol.2014.260 · Cited by 124
YaeL proteolysis of RseA is controlled by the PDZ domain of YaeL and a Gln‐rich region of RseA
Kanehara, K., Ito, K., & Akiyama, Y. (2003) · EMBO Journal · doi:10.1093/emboj/cdg602 · Cited by 117
Ion channel sequestration in central nervous system axons
Rasband, M., & Shrager, P. (2000) · Journal of Physiology · doi:10.1111/j.1469-7793.2000.00063.x · Cited by 117
“The extent of myelination was gauged by double labelling for Na¤ channels and either myelin-associated glycoprotein (MAG) or CasprÏparanodin, a component of the axoglial junctions at paranodes (Einheber et al. 1997; Menegoz et al. 1997; Peles et al. 1997).”
Metadata
- Authors
- Peles, E., Nativ, M., Lustig, M., Grumet, M., Schilling, J., Martinez, R., Plowman, G. D., & Schlessinger, J.
- Affiliations
- NYU Langone Health (US)
- Corresponding author
- Schlessinger, Joseph
- Venue
- The EMBO Journal
- Published
- 1997-03-01
- Volume
- 16
- Issue
- 5
- Pages
- 978-988
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC1169698
- OpenAlex
- W2098584548
- Cited by
- 400
- References
- 0
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 6 · 2023: 6 · 2022: 9 · 2021: 6 · 2020: 13 · 2019: 8 · 2018: 9 · 2017: 9 · 2016: 10 · 2015: 8 · 2014: 15 · 2013: 11 · 2012: 12
- FWCI
- 9.98
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01ns021629-11)
- National Institute of Neurological Disorders and Stroke (NS21629)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Axon Guidance and Neuronal Signaling
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Keywords
- Caspr, contactin, epidermal growth factor-like repeats, SH3 domain binding, neurite outgrowth, intracellular signaling, rat brain
- MeSH terms
- Amino Acid Sequence, Animals, Cell Membrane, Cloning, Molecular, Humans, Immunohistochemistry, Molecular Sequence Data, Nerve Tissue Proteins, Neurons, Protein Binding, Receptors, Cell Surface, Recombinant Fusion Proteins, RNA, Messenger, Tumor Cells, Cultured, Blotting, Western, Signal Transduction, Cell Adhesion Molecules, Neuronal, Gene Expression, Sequence Alignment, src Homology Domains, Rats, Contactins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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