The DOI matches its Crossref record; 37 of the 37 references it cites were found in a registry or an index.
Sodium Channel β Subunits Mediate Homophilic Cell Adhesion and Recruit Ankyrin to Points of Cell-Cell Contact
Open accessAbstract
Sodium channels isolated from mammalian brain are composed of alpha, beta1, and beta2 subunits. The auxiliary beta subunits do not form the ion conducting pore, yet play important roles in channel modulation and plasma membrane expression. beta1 and beta2 are transmembrane proteins with one extracellular V-set immunoglobulin (Ig) protein domain. It has been shown recently that beta1 and beta2 interact with the extracellular matrix proteins tenascin-C and tenascin-R. In the present study we show that rat brain beta1 and beta2, but not alphaIIA, subunits interact in a trans-homophilic fashion, resulting in recruitment of the cytoskeletal protein ankyrin to sites of cell-cell contact in transfected Drosophila S2 cells. Whereas alphaIIA subunits expressed alone do not cause cellular aggregation, beta subunits co-expressed with alphaIIA retain the ability to adhere and recruit ankyrin. Truncated beta subunits lacking cytoplasmic domains interact homophilically to produce cell aggregation but do not recruit ankyrin. Thus, the cytoplasmic domains of beta1 and beta2 are required for cytoskeletal interactions. It is hypothesized that sodium channel beta subunits serve as a critical communication link between the extracellular and intracellular environments of the neuron and may play a role in sodium channel placement at nodes of Ranvier.
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Cites
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Primary structure and functional expression of the beta 1 subunit of the rat brain sodium channel
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Self-citationNeuroligin 1 is a postsynaptic cell-adhesion molecule of excitatory synapses
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Auxiliary subunits of voltage-gated ion channels
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Self-citationBunch, T. A., Grinblat, Y., & Goldstein, L. S. B. (1988) · Nucleic Acids Research · doi:10.1093/nar/16.3.1043 · Cited by 435
Ankyrin and spectrin associate with voltage-dependent sodium channels in brain
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Ion Channels in Presynaptic Nerve Terminals and Control of Transmitter Release
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Cited by
Resurgence of sodium channel research
Goldin, A. L. (2001) · Annual Review of Physiology · doi:10.1146/annurev.physiol.63.1.871 · Cited by 688
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
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Cellular mechanisms of direct-current electric field effects: galvanotaxis and metastatic disease
Mycielska, M. E., & Djamgoz, M. B. A. (2004) · Journal of Cell Science · doi:10.1242/jcs.01125 · Cited by 375
Sodium Channel β Subunits: Anything but Auxiliary
Isom, L. L. (2001) · The Neuroscientist · doi:10.1177/107385840100700108 · Cited by 353
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Metadata
- Authors
- Malhotra, J. D., Kazen-Gillespie, K., Hortsch, M., & Isom, L. L.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-04
- Volume
- 275
- Issue
- 15
- Pages
- 11383-11388
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1968924035
- Cited by
- 272
- References
- 37
- FWCI
- 6.76
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: Sodium Channel β Subunits Mediate Homophilic Cell Adhesion and Recruit Ankyrin to Points of Cell-Cell Contact. https://app.cochat.ai/papers/10.1074/jbc.275.15.11383
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- Malhotra, J. D., Kazen-Gillespie, K., Hortsch, M., & Isom, L. L. (2000). Sodium Channel β Subunits Mediate Homophilic Cell Adhesion and Recruit Ankyrin to Points of Cell-Cell Contact. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.275.15.11383
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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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