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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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Items 201–300 of 385
Internodal specializations of myelinated axons in the central nervous system
Arroyo, E., Xu, T., Poliak, S., Watson, M. R., Peles, E., & Scherer, S. (2001) · Cell and Tissue Research · doi:10.1007/s004410100403 · Cited by 53
“We used rabbit antisera against rat Kv1.1 and Kv1.2 (diluted 1:300; Alomone Labs, Jerusalem, Israel), Caspr (diluted 1:1000; Einheber et al. 1997; Peles et al. 1997 ), Caspr2 (diluted 1:100; Poliak et al. 1999), MAG (diluted 1:300; Pedraza et al. 1990), claudin-11/OSP (dilut- 55”
MethodSelf-citationNew insights into the roles of the contactin cell adhesion molecules in neural development.
Mohebiany, A., Harroch, S., & Bouyain, S. (2014) · Advances in neurobiology · doi:10.1007/978-1-4614-8090-7_8 · Cited by 53
Type 1 Diabetic Neuropathy and C‐peptide
Sima, A. A. F., Zhang, W., & Grunberger, G. (2003) · Journal of Diabetes Research · doi:10.1080/15438600490424541 · Cited by 50
“These are also associated with spectrin, actin, and contactin, which, via β1 Na+ channel subunit and RTPTβ , interact with caspr (Einheber et al., 1997; Menegoz et al., 1997; Peles et al., 1997).”
BackgroundAndrews, N. P., Boeckman, J. X., Manning, C. F., Nguyen, J. T., Bechtold, H., Dumitras, C., Gong, B., Nguyen, K., van der List, D. A., Murray, K. D., et al. (2019) · eLife · doi:10.7554/elife.43322 · Cited by 52
“directed against CASPR, a protein concentrated at paranodes (41, 42).”
BackgroundDevanathan, V., Jakovcevski, I., Santuccione, A., Li, S., Lee, H. J., Peles, E., Leshchyns’ka, I., Sytnyk, V., & Schachner, M. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.5657-09.2010 · Cited by 52
“Caspr also interacts with the receptorlike protein tyrosine phosphatase RTPT (Peles et al., 1997), which induces neurite outgrowth by binding to contactin (Sakurai et al.”
BackgroundMethodInfluentialSelf-citationRevest, J.-M., Faivre-Sarrailh, C., Maeda, N., Noda, M., Schachner, M., & Rougon, G. (1999) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.1999.00521.x · Cited by 52
The regulation of glial-specific splicing ofNeurexin IVrequires HOW and Cdk12 activity
Rodrigues, F., Thuma, L., & Klämbt, C. (2012) · Development · doi:10.1242/dev.074070 · Cited by 46
“Nrx-IV is an evolutionary conserved protein that is also found in the vertebrate nervous system, where it is called Caspr (contactin-associated protein) (Peles et al., 1997a; Peles et al., 1997b).”
BackgroundLei, Y., Xin, X., Morgan, D. K., Pintar, J., & Fricker, L. (1999) · DNA and Cell Biology · doi:10.1089/104454999315565 · Cited by 51
Septate and paranodal junctions: kissing cousins
Hortsch, M., & Margolis, B. L. (2003) · Trends in Cell Biology · doi:10.1016/j.tcb.2003.09.004 · Cited by 46
Xin, X., Day, R., Dong, W., Lei, Y., & Fricker, L. D. (1998) · DNA and Cell Biology · doi:10.1089/dna.1998.17.897 · Cited by 50
“…(Takagi et al, 1991); Dis Dom R, human discoidin domain receptor (Johnson et al, 1993); Caspr, human contactin-associated transmembrane receptor (Peles et al, 1997); and disc-la, discoidin la (Pooler al, 1981). formaldehyde/agarose gel, transferred to nitrocellulose; and probed as described in…”
Chiu, C. G., Nakamura, Y., Chong, K. K., Huang, S. K., Kawas, N. P., Triche, T. J., Elashoff, D. A., Kiyohara, E., Irie, R. F., Morton, D. L., et al. (2014) · Clinical Chemistry · doi:10.1373/clinchem.2013.213611 · Cited by 53
The cytoskeletal adapter protein 4.1G organizes the internodes in peripheral myelinated nerves
Ivanovic, A., Horresh, I., Golan, N., Spiegel, I., Sabanay, H., Frechter, S., Ohno, S., Terada, N., Möbius, W., Rosenbluth, J., et al. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201111127 · Cited by 51
“Antibodies against Necl4 (Spiegel et al., 2007), Caspr (Peles et al., 1997), NF155 (Gollan et al., 2003), and contactin (Rios et al., 2000) have been 343Role of protein 4.1G in myelinating Schwann cells • Ivanovic et al. Golan, N., K. Adamsky, E. Kartvelishvily, D. Brockschnieder, W. Möbius, I.…”
InfluentialSelf-citationWinters, J. J., Ferguson, C., Lenk, G. M., Giger-Mateeva, V. I., Shrager, P. G., Meisler, M. H., & Giger, R. J. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.1482-11.2011 · Cited by 54
“Primary antibodies used were monoclonal anti-pan Na channels (Rasband et al., 1999) and polyclonal anti-Caspr (Peles et al., 1997).”
BackgroundInfluentialTreubert, U., & Brümmendorf, T. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-05-01795.1998 · Cited by 49
Identification of Novel γ-Secretase-associated Proteins in Detergent-resistant Membranes from Brain
Hur, J., Teranishi, Y., Kihara, T., Yamamoto, N. G., Inoue, M., Hosia, W., Hashimoto, M., Winblad, B. G., Frykman, S., & Tjernberg, L. O. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.246074 · Cited by 51
“Contactin-associated protein 1 (CNTNAP1 as gene symbol, Caspr, Neurexin IV, or Paranodin as protein name) is a transmembrane protein that forms a cisinteraction with the glycosylphosphatidylinositol-anchored protein contactin (57).”
BackgroundKatidou, M., Vidaki, M., Strigini, M., & Karagogeos, D. (2008) · Biotechnology Journal · doi:10.1002/biot.200800281 · Cited by 43
“In addition, Nf155 (via the Nf155/Caspr/Contactin adhesion complex) promotes the migration of oligodendrocyte processes on CNS axons, which is required for effective myelination [94].”
BackgroundInfluentialHoshi, T., Suzuki, A., Hayashi, S., Tohyama, K., Hayashi, A., Yamaguchi, Y., Takeuchi, K., & Baba, H. (2007) · Glia · doi:10.1002/glia.20487 · Cited by 48
“The polyclonal anti-Caspr antibody, a kind gift of Dr. Peles (The Weizmann Institute of Science, Rehovot, Israel), was used at a dilution of 1:1,500 (Peles et al., 1997).”
MethodMyelination and Regional Domain Differentiation of the Axon
Thaxton, C., & Bhat, M. A. (2009) · Results and problems in cell differentiation · doi:10.1007/400_2009_3 · Cited by 48
“Contactin is also enriched at the paranodes of myelinated fibers and forms a cis interaction with Caspr in the axolemma (Peles et al. 1997; Reid et al. 1994).”
BackgroundSpatial constraints dictate glial territories at murine neuromuscular junctions
Brill, M. S., Lichtman, J. W., Thompson, W. J., Zuo, Y., & Misgeld, T. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201108005 · Cited by 47
“The anti-Caspr antibody (a gift from E. Peles, Weizmann Institute of Science, Rehovot, Israel; Peles et al., 1997) was used at a concentration of 1:800 in 0.2% Triton X-100 and 1% BSA in PBS followed by incubation with appropriate secondary antibodies in PBS. Entire triangularis sterni muscles and thin layers dissecte…”
MethodInfluentialGallego-Delgado, P., James, R., Browne, E., Meng, J., Umashankar, S., Tan, L. Y., Picón, C., Mazarakis, N. D., Faisal, A. A., Howell, O. W., et al. (2020) · PLoS Biology · doi:10.1371/journal.pbio.3001008 · Cited by 58
Cell adhesion molecules in the CNS
Sakisaka, T., & Takai, Y. (2005) · Journal of Cell Science · doi:10.1242/jcs.02672 · Cited by 45
“At the paranode, the transmembrane protein Caspr is found on the axon surface in association with the GPIanchored cell adhesion molecule contactin (Peles et al., 1997).”
BackgroundWart, A. V., Boiko, T., Trimmer, J., & Matthews, G. (2005) · Molecular and cellular neurosciences · doi:10.1016/j.mcn.2004.11.012 · Cited by 45
“Rabbit polyclonal anti-Caspr antibodies (Boiko et al., 2001) were made against the same fusion protein as previously characterized anti-Caspr rabbit polyclonal antibodies (Peles et al., 1997).”
BackgroundCellular junctions of myelinated nerves (Review)
Spiegel, I., & Peles, E. (2002) · Molecular membrane biology · doi:10.1080/09687680210130009 · Cited by 45
“Within the neurexin superfamily, Caspr belongs to a distinct subgroup (named also NCP; Bellen et al. 1998), which contains five distinct genes (Caspr-Caspr5 (Peles et al. 1997, Poliak et al. 1999, Spiegel et al. 2002)).”
BackgroundInfluentialSelf-citationCaspr and Caspr2 Are Required for Both Radial and Longitudinal Organization of Myelinated Axons
Gordon, A., Adamsky, K., Vainshtein, A., Frechter, S., Dupree, J., Rosenbluth, J., & Peles, E. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.3369-14.2014 · Cited by 43
“, 2002), Caspr (Peles et al., 1997), Caspr2 (Poliak et al.”
BackgroundSelf-citationTan, R., Leshchyns’ka, I., & Sytnyk, V. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00378 · Cited by 42
“For example, IgLON protein family members with three Ig domains contain six or seven N-glycosylation sites in their ectodomains (Figure 1; Pimenta et al., 1996; Itoh et al., 2008).”
BackgroundSun, X.-Y., Takagishi, Y., Okabe, E., Chishima, Y., Kanou, Y., Murase, S., Mizumura, K., Inaba, M., Komatsu, Y., Hayashi, Y., et al. (2009) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/nen.0b013e3181be2e96 · Cited by 42
“The following antibodies were used: affinity-purified mouse monoclonal and rabbit polyclonal antibodies to Caspr (1:200 and 1:2000) (25, 26); mouse anti-contactin (BD Biosciences); rabbit antiNF155 (a gift of H.”
MethodSelf-citationGersten, M. J., Alirezaei, M., Marcondes, M. C. G., Flynn, C. T., Ravasi, T., Ideker, T., & Fox, H. S. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.3180-09.2009 · Cited by 43
“CNTNAP1 (M9644) is a transmembrane protein which may act as a signaling subunit of contactin (Peles et al., 1997) and is required, together with contactin, for normal organization of paranodal junctions between glia and axons in myelinated fibers (Bhat et al.”
BackgroundInfluentialRasband, M., Taylor, C. M., & Bansal, R. (2003) · Glia · doi:10.1002/glia.10284 · Cited by 42
“Rabbit polyclonal antibodies were made against a Caspr fusion protein kindly provided by Dr. Elior Peles (Peles et al., 1997).”
MethodAssociation of Cell Adhesion Molecules Contactin-6 and Latrophilin-1 Regulates Neuronal Apoptosis
Zuko, A., Oguro‐Ando, A., Post, H., Taggenbrock, R. L. R. E., van Dijk, R. E., Altelaar, M. A. F., Heck, A. J. R., Petrenko, A. G., van der Zwaag, B., Shimoda, Y., et al. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00143 · Cited by 36
“…of Cntn1 and Cntn2, the best studied members of the contactin family involves the formation of multiple homo- and heterodimers in both cis and transconfigurations that are essential for the structure of the paranode and juxtaparanode (Peles et al., 1997; Rios et al., 2000; Poliak et al., 2003).”
BackgroundWhitehouse, I. J., Miners, J. S., Glennon, E. B. C., Kehoe, P. G., Love, S., Kellett, K. A. B., & Hooper, N. M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0059554 · Cited by 43
“The subcellular locations of contactin proteins are tightly regulated by their post-translational processing and interactions with contactin-associated proteins [29,30,31].”
BackgroundFuchs, P., Zörer, M., Reipert, S., Rezniczek, G. A., Propst, F., Walko, G., Fischer, I., Bauer, J., Leschnik, M., Lüscher, B., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.018150 · Cited by 41
Parent, A., Mungenast, A., Lomniczi, A., Sandau, U., Peles, E., Bosch, M., Rønnekleiv, O., & Ojeda, S. (2007) · Journal of neuroendocrinology · doi:10.1111/j.1365-2826.2007.01597.x · Cited by 40
Self-citationEffect of an R69C mutation in the myelin protein zero gene on myelination and ion channel subtypes.
Bai, Y.-H., Ianokova, E., Pu, Q., Ghandour, K., Levinson, R., Martin, J.-J., Groote, C. C.-D., Mazanec, R., Seeman, P., Shy, M., et al. (2006) · Archives of Neurology · doi:10.1001/archneur.63.12.1787 · Cited by 40
Poon, M. M., Lorrain, K. I., Stebbins, K. J., Edu, G. C., Broadhead, A. R., Lorenzana, A. O., Roppe, J. R., Baccei, J., Baccei, C. S., Chen, A. C., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2407974121 · Cited by 42
“Upon myelination, nodal marker proteins like Caspr cluster in the axon (25).”
BackgroundDenisenko‐Nehrbass, N., Goutebroze, L., Galvez, T., Bonnon, C., Stankoff, B., Ezan, P., Giovannini, M., Faivre-Sarrailh, C., & Girault, J. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01503.x · Cited by 39
“The short intracellular region of paranodin contains a C-terminal proline-rich region that may interact with Src homology 3 (SH3)-containing proteins (Peles et al. 1997).”
BackgroundInfluentialKv7.2 regulates the function of peripheral sensory neurons
King, C. H., Lancaster, E., Salomon, D., Peles, E., & Scherer, S. S. (2014) · The Journal of Comparative Neurology · doi:10.1002/cne.23595 · Cited by 44
“The mouse monoclonal contactin-associated protein (Caspr) antiserum (Peles et al., 1997; catalog No. contactin-associated protein [Caspr], RRID:AB_2311776) was generated by Dr. Poliak by immunizing mice with a fusion protein composed of the extracellular domain of human Caspr (amino acids 1–1282;…”
MethodSelf-citationMorris, R., Cox, H., Mombelli, E., & Quinn, P. (2004) · Sub-cellular biochemistry · doi:10.1007/978-1-4757-5806-1_2 · Cited by 38
Receptor protein-tyrosine phosphatase signalling in development.
den Hertog, J., Blanchetot, C., Buist, A., Overvoorde, J., van der Sar, A. M., & Tertoolen, L. (1999) · International Journal of Developmental Biology · doi:10.1387/ijdb.10668981 · Cited by 38
Ogawa, Y., Lim, B. C., George, S., Osés-Prieto, J. A., Rasband, J. M., Eshed‐Eisenbach, Y., Hamdan, H., Nair, S., Boato, F., Peles, E., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42273-8 · Cited by 48
Self-citationThe Interaction Between Contactin and Amyloid Precursor Protein and Its Role in Alzheimer’s Disease
Bamford, R. A., Widagdo, J., Takamura, N., Eve, M., Anggono, V., & Oguro‐Ando, A. (2019) · Neuroscience · doi:10.1016/j.neuroscience.2019.10.006 · Cited by 47
Arabinogalactan Proteins: Involvement in Plant Growth and Morphogenesis
Rumyantseva, N. I. (2005) · Biochemistry (Moscow) · doi:10.1007/s10541-005-0228-7 · Cited by 37
Upregulation of Tyrosine Kinase TKT by the Epstein-Barr Virus Transactivator Zta
Lu, J., Chen, S.-Y., Chua, H.-H., Liu, Y.-S., Huang, Y.-T., Chang, Y., Chen, J.-Y. Y., Sheen, T., & Tsai, C.-H. (2000) · Journal of Virology · doi:10.1128/jvi.74.16.7391-7399.2000 · Cited by 37
“For example, neurexin, which has a discoidin I domain, is believed to participate in neuron-glial cell adhesion ( 38 ).”
BackgroundContactin is expressed in human astrocytic gliomas and mediates repulsive effects
Eckerich, C., Zapf, S., Ulbricht, U., Müller, S., Fillbrandt, R., Westphal, M., & Lamszus, K. (2006) · Glia · doi:10.1002/glia.20254 · Cited by 36
“Binding of astroglial PTPf to contactin on the surface of neuronal cells promotes neurite growth and neuronal differentiation, and both molecules are important mediators of glial–neuronal crosstalk (Peles et al., 1997; Sakurai et al., 1997; Revest et al., 1999; Virgintino et al., 1999).”
BackgroundKwon, H., Nakaya, N., Abu-Asab, M., Kim, H.-S., & Tomarev, S. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.4731-13.2014 · Cited by 35
“In the optic nerve, myocilin is not concentrated at nodes of Ranvier as shown by immunostaining of the longitudinal sections of the optic nerve with antibodies against myocilin and perinodal marker Caspr (Menegoz et al., 1997, Peles et al., 1997; Fig.”
BackgroundNew members of the neurexin superfamily: multiple rodent homologues of the human CASPR5 gene
Traut, W., Weichenhan, D., Himmelbauer, H., & Winking, H. (2006) · Mammalian Genome · doi:10.1007/s00335-005-0157-1 · Cited by 35
“Caspr1 (contactin associated protein = Caspr = CNTNAP1) and Caspr2-4 (contactin-associated protein-like 2 4) are predominantly found in nerve tissue (Peles et al. 1997; Poliak et al. 1999; Spiegel et al. 2002).”
BackgroundZacharias, U., Nörenberg, U., & Rathjen, F. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.34.24357 · Cited by 35
Assembly of CNS Nodes of Ranvier in Myelinated Nerves Is Promoted by the Axon Cytoskeleton
Brivio, V., Faivre-Sarrailh, C., Peles, E., Sherman, D., & Brophy, P. (2017) · Current Biology · doi:10.1016/j.cub.2017.01.025 · Cited by 34
Self-citationComparing peripheral glial cell differentiation in Drosophila and vertebrates
Rodrigues, F., Schmidt, I., & Klämbt, C. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0512-6 · Cited by 33
“Axonal Caspr and 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 [80–87].”
Tong, D.-L., Chen, R.-G., Lu, Y.-L., Li, W.-K., Zhang, Y.-F., Lin, J.-K., He, L.-J., Dang, T., Shan, S., Xu, X.-H., et al. (2018) · bioRxiv · doi:10.1101/260083 · Cited by 33
Santos, S. D., Iuliano, O., Ribeiro, L. F., Veran, J., Ferreira, J. S., Rio, P., Mulle, C., Duarte, C. B., & Carvalho, A. L. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.322909 · Cited by 30
“1-band proteins and a proline-rich sequence (16, 17).”
BackgroundA Comparative Perspective on Wnt/β-Catenin Signalling in Cell Fate Determination
Garcin, C. L., & Habib, S. J. (2017) · Results and problems in cell differentiation · doi:10.1007/978-3-319-53150-2_15 · Cited by 40
Keratan Sulfate Proteoglycan Phosphacan Regulates Mossy Fiber Outgrowth and Regeneration
Butler, C., Schnetz, S. A., Yu, E., Davis, J. B., Temple, K., Silver, J., & Malouf, A. T. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.3040-03.2004 · Cited by 32
“…work of the Schlessinger and Grumet labs, which provided strong evidence that RPTP/ expressed on astrocytes interacts with contactin expressed on neuronal cells and that this interaction between the astrocytes and neurons can alter axon outgrowth (Peles et al., 1995, 1997; Sakurai et al., 1997).”
BackgroundExpression of discoidin domain receptor 1 tyrosine kinase on the human bronchial epithelium.
Sakamoto, O., Suga, M., Suda, T., & Ando, M. (2001) · European Respiratory Journal · doi:10.1183/09031936.01.17509690 · Cited by 32
“In addition, discoidin-I domains are homologous to the constant regions of blood coagulation cofactors V and VIII [16] and to neuropilins and neurexins, which are involved in the development of the nervous system [17, 18].”
Molecular constituents of the node of ranvier
Kazarinova-Noyes, K., & Shrager, P. (2002) · Molecular Neurobiology · doi:10.1385/mn:26:2-3:167 · Cited by 31
“Studies were greatly accelerated by the discovery of caspr/paranodin, a neurexin-family membrane protein which is present at high density at paranodes (44,45), and which has been shown to form part of the axo-glial junctions at that site (31).”
BackgroundGlycosyl-phosphatidylinositol-anchor addition signals are processed in Nicotiana tabacum.
Takos, A. M., Dry, I., & Soole, K. (2000) · The Plant Journal · doi:10.1046/j.1365-313x.2000.00651.x · Cited by 31
Identification of synaptic plasma membrane proteins co‐precipitated with fibrillar β‐amyloid peptide
Verdier, Y., Huszár, E., Penke, B., Penke, Z., Woffendin, G., Ščigelová, M., Fülöp, L., Szűcs, M., Medzihradszky, K. F., & Janáky, T. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03158.x · Cited by 30
“(3) Neuronal cell adhesion molecules: contactin 1 (Hosoya et al. 1995), contactin-associated protein 1 precursor (Peles et al. 1997), flotillin-1 (Lang et al. 1998), neurotrimin (Struyk et al. 1995), opioid-binding cell adhesion molecule (Miyata et al. 2003), gap junction a-1 protein (Dupont et al.…”
BackgroundDeciphering the Function of Neurexins at Cellular Junctions
Littleton, J. T., Bhat, M., & Bellen, H. J. (1997) · Journal of Cell Biology · doi:10.1083/jcb.137.4.793 · Cited by 30
Franco-Pons, N., Virgos, C., Vogel, W. F., Ureña, J. M., Soriano, E., del Río, J. D., & Vilella, E. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2006.02.033 · Cited by 30
Jones, J. M., Dionne, L. A., Dell'Orco, J. M., Parent, R., Krueger, J. N., Cheng, X.-Y., Dib-Hajj, S., Bunton-Stasyshyn, R., Sharkey, L., Dowling, J., et al. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.01.018 · Cited by 29
Zhang, Y., Yang, J., & Showalter, A. M. (2011) · Plant Signalling & Behavior · doi:10.4161/psb.6.6.15204 · Cited by 29
Axon kinematics change during growth and development.
Hao, H., & Shreiber, D. (2007) · Journal of Biomechanical Engineering · doi:10.1115/1.2746372 · Cited by 29
Suzuki, A., Hoshi, T., Ishibashi, T., Hayashi, A., Yamaguchi, Y., & Baba, H. (2004) · Glia · doi:10.1002/glia.20008 · Cited by 29
“For instance, receptor-type tyrosine phosphatase (RPTP ) is present both in glia and the axon at the nodes and is a ligand for the axonal cell recognition molecule contactin (Peles et al., 1995, 1997; Ratcliffe et al., 2000).”
BackgroundMethodInfluentialGilson, P., Gaspar, Y. M., Oxley, D., Youl, J., & Bacic, A. (2005) · Protoplasma · doi:10.1007/bf01280309 · Cited by 29
“Alternatively, membrane-bound AGPs may interact with putative transmembrane receptors as occurs in animal cell-to-cell interactions (Peles et al. 1997).”
BackgroundDifferential Contribution of Cadm1–Cadm3 Cell Adhesion Molecules to Peripheral Myelinated Axons
Sukhanov, N., Vainshtein, A., Eshed‐Eisenbach, Y., & Peles, E. (2021) · Journal of Neuroscience · doi:10.1523/jneurosci.2736-20.2020 · Cited by 31
“Antibodies The following primary antibodies were used: rat anti-neurofilament (NF-H; MAB5448, Millipore Bioscience Research Reagents), chicken anti-NF-H (AB_2313552 AVES labs), rabbit anti-Caspr (Peles et al., 1997), rabbit anti- Kv1.”
MethodSelf-citationHirata, H., Takahashi, A., Shimoda, Y., & Koide, T. (2016) · PLoS ONE · doi:10.1371/journal.pone.0147887 · Cited by 39
Kruger, R., Goodyear, R., Legan, P., Warchol, M. E., Raphael, Y., Cotanche, D., & Richardson, G. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-12-04815.1999 · Cited by 28
“…interacts with a complex composed of contactin, Nr CAM, and the contactin-associated protein caspr (Peles et al., 1995; Sakurai et al., 1997; Peles et al., 1997; for review, see Peles et al., 1998), and the laminin-nidogen complex can act as a ligand for the leukocyte common antigen-related…”
BackgroundDifferential clustering of Caspr by oligodendrocytes and Schwann cells
Eisenbach, M., Kartvelishvily, E., Eshed-Eisenbach, Y., Watkins, T. A., Sorensen, A., Thomson, C., Ranscht, B., Barnett, S. C., Brophy, P., & Peles, E. (2009) · Journal of Neuroscience Research · doi:10.1002/jnr.22157 · Cited by 27
“Polyclonal antibodies used included Caspr (1:1,000; Peles et al., 1997) and NF-155 (1:100; Tait et al., 2000).”
BackgroundMethodSelf-citationLakhani, S., Doan, R. N., Al‐Mureikhi, M., Partlow, J. N., Al‐Saffar, M., Elsaid, M. F., Alaaraj, N., Barkovich, A. J., Walsh, C. A., & Ben‐Omran, T. (2017) · European Journal of Medical Genetics · doi:10.1016/j.ejmg.2017.02.006 · Cited by 28
“The CNTNAP1 gene encodes the anchorage protein CASPR, which consists of extracellular, helical (transmembrane), and cytoplasmic regions (Peles et al., 1997).”
BackgroundMethodInfluentialHolland, S., Peles, E., Pawson, T., & Schlessinger, J. (1998) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(98)80015-9 · Cited by 26
Self-citationRegulation of Signaling by Protein-Tyrosine Phosphatases: Potential Roles in the Nervous System
Arregui, C., Balsamo, J., & Lilien, J. (2004) · Neurochemical Research · doi:10.1023/a:1007595617447 · Cited by 26
“PTP β is also expressed on the surface of the glial cells (90,91) and may play a role in axonal growth and neuronal migration by binding to neuronal receptors such as contactin, the neurexin-like protein Caspr, N-CAM and NrCAM (homologue of Ng-CAM) (83,92).”
BackgroundColom, B., Poitelon, Y., Huang, W., Woodfin, A., Averill, S., Carro, U. D., Zambroni, D., Brain, S. D., Perretti, M., Ahluwalia, A., et al. (2011) · The FASEB Journal · doi:10.1096/fj.11-196220 · Cited by 24
Babiarz, J., Kane-Goldsmith, N., Basak, S. M., Liu, K., Young, W., & Grumet, M. (2011) · Experimental Neurology · doi:10.1016/j.expneurol.2010.08.028 · Cited by 25
“Caspr, which is expressed diffusely on unmyelinated neurons, clustered at nodes and hemi-nodes in the myelinating co-cultures with Schwann cells (Einheber et al., 1997; Peles et al., 1997) and P12 OEC (Fig.”
BackgroundSelf-citationLafont, D., Adage, T., Gréco, B., & Zaratin, P. (2009) · Behavioural Brain Research · doi:10.1016/j.bbr.2009.01.025 · Cited by 25
Fibronectin is a binding partner for the myelin‐associated glycoprotein (siglec‐4a)
Strenge, K., Brossmer, R., Ihrig, P., Schauer, R., & Kelm, S. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02566-2 · Cited by 25
The beneficial effects of C-Peptide on diabetic polyneuropathy.
Kamiya, H., Zhang, W., & Sima, A. (2009) · The review of diabetic studies : RDS · doi:10.1900/rds.2009.6.187 · Cited by 25
“The β-subunits also interact with RPTP-β, a ligand for the neuronal receptor contactin [107-109] (Figure 5).”
BackgroundInfluentialMungenast, A. E., & Ojeda, S. (2005) · Journal of Neuroendocrinology · doi:10.1111/j.1365-2826.2005.01293.x · Cited by 22
Fashena, S., & Zinn, K. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.12.6859 · Cited by 24
Structure and evolution of neuronal wiring receptors and ligands
Cortés, E. C., Pak, J. S., & Özkan, E. (2022) · Developmental Dynamics · doi:10.1002/dvdy.512 · Cited by 25
Oligodendroglial Lineage Cells in Thyroid Hormone-Deprived Conditions
Kim, M. J., & Petratos, S. (2019) · Stem Cells International · doi:10.1155/2019/5496891 · Cited by 24
Transmembrane scaffolding proteins in the formation and stability of nodes of Ranvier
Girault, J., Oguievetskaia, K., Carnaud, M., Denisenko‐Nehrbass, N., & Goutebroze, L. (2003) · Biology of the Cell · doi:10.1016/s0248-4900(03)00073-x · Cited by 23
“Paranodin forms a complex with contactin, a glycosyl-phosphatidylinositol-anchored protein of the immunoglobulin-like cell adhesion molecule superfamily (Menegoz et al., 1997; Peles et al., 1997).”
BackgroundCarpita, N., Campbell, M., & Tierney, M. (2001) · Springer Netherlands · doi:10.1007/978-94-010-0668-2 · Cited by 23
Lomniczi, A., & Ojeda, S. R. (2008) · Springer eBooks · doi:10.1007/978-0-387-79492-1_19 · Cited by 25
Pillai, A., Garcia-Fresco, G. P., Sousa, A. D., Dupree, J. L., Philpot, B. D., & Bhat, M. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21374 · Cited by 22
“Caspr interacts with Cont in cis, and Cont is required for the cell surface delivery of Caspr (Peles et al., 1997; Faivre-Sarrailh et al., 2000).”
BackgroundMicroscopic anatomy: normal structure.
King, R. (2013) · Handbook of Clinical Neurology · doi:10.1016/b978-0-444-52902-2.00002-3 · Cited by 22
Kamasawa, N., Attila Gabor, S. I. K., Morita, M., Yasumura, T., Davidson, K. G. V., Nagy, J. I., & Rash, J. E. (2005) · Neuroscience · doi:10.1016/j.neuroscience.2005.08.027 · Cited by 178
“The protein caspr is selectively concentrated in paranodal regions at nodes of Ranvier (Einheber et al., 1997; Peles et al., 2005).”
Structural insights into the contactin 1 – neurofascin 155 adhesion complex
Chataigner, L., Gogou, C., den Boer, M. A., Frias, C. P., Thies-Weesie, D., Granneman, J., Heck, A., Meijer, D., & Janssen, B. (2022) · Nature Communications · doi:10.1038/s41467-022-34302-9 · Cited by 21
Chang, K.-J., Agrawal, I., Vainshtein, A., Ho, W. Y., Xin, W., Tucker‐Kellogg, G., Susuki, K., Peles, E., Ling, S., & Chan, J. R. (2021) · eLife · doi:10.7554/elife.64456 · Cited by 22
Self-citationGenomic organization and expression properties of the VfENOD5 gene from broad bean (Vicia faba L.).
Frühling, M., Hohnjec, N., Schröder, G., Küster, H., Pühler, A., & Perlick, A. M. (2000) · Plant Science · doi:10.1016/s0168-9452(00)00216-8 · Cited by 21
Nizon, M., Cogné, B., Vallat, J., Joubert, M., Liet, J., Simon, L., Vincent, M., Küry, S., Boisseau, P., Schmitt, S., et al. (2016) · European Journal of Human Genetics · doi:10.1038/ejhg.2016.142 · Cited by 20
Kirrbach, J., Krugliak, M., Ried, C., Pagel, P., Arkin, I., & Langosch, D. (2013) · Bioinform. · doi:10.1093/bioinformatics/btt247 · Cited by 20
Proteomic analysis of the presynaptic active zone
Volknandt, W., & Karas, M. (2012) · Experimental Brain Research · doi:10.1007/s00221-012-3031-x · Cited by 24
Mierzwa, A. J., Arévalo, J., Schiff, R., Chao, M. V., & Rosenbluth, J. (2010) · The Journal of comparative neurology · doi:10.1002/cne.22367 · Cited by 20
“Caspr antiserum recognized only a single band (190 kDa) on Western blots of mouse brain in a similar fashion as previous reports (Peles et al., 1997).”
ResultThe mouse F3/contactin glycoprotein
Bizzoca, A., Corsi, P., & Gennarini, G. (2009) · Cell Adhesion & Migration · doi:10.4161/cam.3.1.7462 · Cited by 20
Molecular organization of the nodal region is not altered in spontaneously diabetic BB‐Wistar rats
Brown, A. A., Xu, T., Arroyo, E., Levinson, S., Brophy, P., Peles, E., & Scherer, S. S. (2001) · Journal of Neuroscience Research · doi:10.1002/jnr.1137 · Cited by 20
“Caspr was originally discovered owing to its cis interaction with contactin (Peles et al., 1997), and Rios et al.”
BackgroundSelf-citationMutations of CNTNAP1 led to defects in neuronal development
Li, W., Yang, L., Tang, C., Liu, K., Lu, Y., Wang, H., Yan, K., Qiu, Z., & Zhou, W. (2020) · JCI Insight · doi:10.1172/jci.insight.135697 · Cited by 23
“bind Cntn1 (13, 14), neurofascin (2, 15, 16), and native prion protein (17), which are involved in neurite outgrowth (18), neuronal migration (19), dendritic branching (20, 21), and synaptogenesis (22), thereby allowing inferences about its potential functions in early brain development.”
BackgroundInfluentialHuang, J. K., Ferrari, C. C., de Castro, G. M., Lafont, D., Zhao, C., Zaratin, P., Pouly, S., Greco, B. M., & Franklin, R. J. M. (2012) · American Journal Of Pathology · doi:10.1016/j.ajpath.2012.07.011 · Cited by 19
Nogo signaling and non‐physical injury‐induced nervous system pathology
Teng, F., & Tang, B. L. (2005) · Journal of Neuroscience Research · doi:10.1002/jnr.20361 · Cited by 19
“(2003) have shown that Nogo-A seems to interact with the adhesion molecule Caspr/paranodin (Peles et al., 1997) and also indirectly with Caspr-associated potassium channels (Bhat et al.”
BackgroundRole of CD21 antigen in diffuse large B‐cell lymphoma and its clinical significance
Otsuka, M., Yakushijin, Y., Hamada, M., Hato, T., Yasukawa, M., & Fujita, S. (2004) · British Journal of Haematology · doi:10.1111/j.1365-2141.2004.05226.x · Cited by 19
“Total RNAs from cell lines were size-fractionated in 1% agarose/formaldehyde gels and transferred to nylon membranes, as described (Peles et al, 1997).”
MethodGPI-Anchored Proteins and Glycosphingolipid-Rich Rafts: Platforms for Adhesion and Signaling
Trotter, J., Klein, C., & Krämer, E. (2000) · The Neuroscientist · doi:10.1177/107385840000600410 · Cited by 19
Christow, S. P., Bychkov, R., Schroeder, C., Dietz, R., Haller, H., Dumler, I., & Gulba, D. C. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00729.x · Cited by 19
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
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