The N-terminal domain of slack determines the formation and trafficking of slick/slack heteromeric sodium-activated potassium channels

Haijun Chen, Jack Kronengold, Yangyang Yan, Valeswara Rao Gazula, Maile R. Brown, Liqun Ma, Gonzalo Ferreira, Youshan Yang, Arin Bhattacharjee, Fred J. Sigworth, Larry Salkoff, Leonard K. Kaczmarek

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Abstract

Potassium channels activated by intracellular Na+ ions (K Na) play several distinct roles in regulating the firing patterns of neurons, and, at the single channel level, their properties are quite diverse. Two known genes, Slick and Slack, encode KNa channels. We have now found that Slick and Slack subunits coassemble to form heteromeric channels that differ from the homomers in their unitary conductance, kinetic behavior, subcellular localization, and response to activation of protein kinase C. Heteromer formation requires the N-terminal domain of Slack-B, one of the alternative splice variants of the Slack channel. This cytoplasmic N-terminal domain of Slack-B also facilitates the localization of heteromeric K Na channels to the plasma membrane. Immunocytochemical studies indicate that Slick and Slack-B subunits are coexpressed in many central neurons. Our findings provide a molecular explanation for some of the diversity in reported properties of neuronal KNa channels.

Original languageEnglish
Pages (from-to)5654-5665
Number of pages12
JournalJournal of Neuroscience
Volume29
Issue number17
DOIs
StatePublished - Apr 29 2009

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    Chen, H., Kronengold, J., Yan, Y., Gazula, V. R., Brown, M. R., Ma, L., Ferreira, G., Yang, Y., Bhattacharjee, A., Sigworth, F. J., Salkoff, L., & Kaczmarek, L. K. (2009). The N-terminal domain of slack determines the formation and trafficking of slick/slack heteromeric sodium-activated potassium channels. Journal of Neuroscience, 29(17), 5654-5665. https://doi.org/10.1523/JNEUROSCI.5978-08.2009