title: The N-terminal domain of Slack determines the formation and trafficking of Slick/Slack heteromeric sodium-activated potassium channels.
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 K(Na) 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 K(Na) channels.
authors.affiliation: Department of Biological Sciences, State University of New York at Albany, Albany, New York 12222, USA.
authors.forename: Haijun
authors.initials: H
authors.lastname: Chen
authors.forename: Jack
authors.initials: J
authors.lastname: Kronengold
authors.forename: Yangyang
authors.initials: Y
authors.lastname: Yan
authors.forename: Valeswara-Rao
authors.initials: VR
authors.lastname: Gazula
authors.forename: Maile R
authors.initials: MR
authors.lastname: Brown
authors.forename: Liqun
authors.initials: L
authors.lastname: Ma
authors.forename: Gonzalo
authors.initials: G
authors.lastname: Ferreira
authors.forename: Youshan
authors.initials: Y
authors.lastname: Yang
authors.forename: Arin
authors.initials: A
authors.lastname: Bhattacharjee
authors.forename: Fred J
authors.initials: FJ
authors.lastname: Sigworth
authors.forename: Larry
authors.initials: L
authors.lastname: Salkoff
authors.forename: Leonard K
authors.initials: LK
authors.lastname: Kaczmarek
mesh_terms: D017398:Alternative Splicing / Q000235:genetics; D000818:Animals; D002460:Cell Line; D005260:Female; D006801:Humans; D009419:Nerve Tissue Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*; D015221:Potassium Channels / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*; D000081033:Potassium Channels, Sodium-Activated; D020033:Protein Isoforms / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D017434:Protein Structure, Tertiary / Q000235:genetics / Q000502:physiology; D021381:Protein Transport / Q000235:genetics / Q000502:physiology; D051381:Rats; D014982:Xenopus laevis
chemical_list: C480493:Kcnt2 potassium channel, rat; D009419:Nerve Tissue Proteins; D015221:Potassium Channels; D000081033:Potassium Channels, Sodium-Activated; D020033:Protein Isoforms; C000626167:kcnt1 protein, rat