The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Contactin Associates with Na+Channels and Increases Their Functional Expression
Open accessAbstract
Contactin (also known as F3, F11) is a surface glycoprotein that has significant homology with the beta2 subunit of voltage-gated Na(+) channels. Contactin and Na(+) channels can be reciprocally coimmunoprecipitated from brain homogenates, indicating association within a complex. Cells cotransfected with Na(+) channel Na(v)1.2alpha and beta1 subunits and contactin have threefold to fourfold higher peak Na(+) currents than cells with Na(v)1.2alpha alone, Na(v)1.2/beta1, Na(v)1.2/contactin, or Na(v)1.2/beta1/beta2. These cells also have a correspondingly higher saxitoxin binding, suggesting an increased Na(+) channel surface membrane density. Coimmunoprecipitation of different subunits from cell lines shows that contactin interacts specifically with the beta1 subunit. In the PNS, immunocytochemical studies show a transient colocalization of contactin and Na(+) channels at new nodes of Ranvier forming during remyelination. In the CNS, there is a particularly high level of colocalization of Na(+) channels and contactin at nodes both during development and in the adult. Contactin may thus significantly influence the functional expression and distribution of Na(+) channels in neurons.
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Peles, E., Nativ, M., Lustig, M., Grumet, M., Schilling, J., Martinez, R., Plowman, G. D., & Schlessinger, J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.5.978 · Cited by 400 · cited 1×
“…(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…”
BackgroundDependence 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. (1999) · The Journal of Neuroscience · doi:10.1523/jneurosci.19-17-07516.1999 · Cited by 325
Self-citationA sodium channel signaling complex: modulation by associated receptor protein tyrosine phosphatase β
Ratcliffe, C. F., Qu, Y., McCormick, K. A., Tibbs, V. C., Dixon, J. E., Scheuer, T., & Catterall, W. A. (2000) · Nature Neuroscience · doi:10.1038/74805 · Cited by 182
Bennett, V., & Lambert, S. (1999) · Journal of Neurocytology · doi:10.1023/a:1007005528505 · Cited by 109
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Voltage-Gated Sodium Channel Expression and Potentiation of Human Breast Cancer Metastasis
Fraser, S. P., Diss, J. K. J., Chioni, A.-M., Mycielska, M. E., Pan, H., Yamaci, R. F., Pani, F., Siwy, Z., Krasowska, M., Grzywna, Z., et al. (2005) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-05-0327 · Cited by 481
Multiple sodium channels and their roles in electrogenesis within dorsal root ganglion neurons
Rush, A. M., Cummins, T. R., & Waxman, S. G. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2006.121483 · Cited by 425
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Metadata
- Authors
- Kazarinova-Noyes, K., Malhotra, J. D., McEwen, D. P., Mattei, L. N., Berglund, E. O., Ranscht, B., Levinson, S. R., Schachner, M., Shrager, P., Isom, L. L., & Xiao, Z.-C.
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2001-10-01
- Volume
- 21
- Issue
- 19
- Pages
- 7517-7525
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- OpenAlex
- W1888714757
- Cited by
- 179
- References
- 4
- FWCI
- 4.13
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Kazarinova-Noyes, K., Malhotra, J. D., McEwen, D. P., Mattei, L. N., Berglund, E. O., Ranscht, B., Levinson, S. R., Schachner, M., Shrager, P., Isom, L. L., & Xiao, Z.-C. (2001). Contactin Associates with Na+Channels and Increases Their Functional Expression. The Journal of Neuroscience. https://doi.org/10.1523/jneurosci.21-19-07517.2001
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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