MinK, MiRP1, and MiRP2 diversify Kv3.1 and Kv3.2 potassium channel gating

Anthony Lewis, Z. McCrossan, G. Abbott

    Research output: Contribution to journalArticlepeer-review

    Abstract

    High frequency firing in mammalian neurons requires ultra-rapid delayed rectifier potassium currents generated by homomeric or heteromeric assemblies of Kv3.1 and Kv3.2 potassium channel α subunits. Kv3.1 α subunits can also form slower activating channels by coassembling with MinK-related peptide 2 (MiRP2), a single transmembrane domain potassium channel ancillary subunit. Here, using channel subunits cloned from rat and expressed in Chinese hamster ovary cells, we show that modulation by MinK, MiRP1, and MiRP2 is a general mechanism for slowing of Kv3.1 and Kv3.2 channel activation and deactivation and acceleration of inactivation, creating a functionally diverse range of channel complexes. MiRP1 also negatively shifts the voltage dependence of Kv3.1 and Kv3.2 channel activation. Furthermore, MinK, MiRP1, and MiRP2 each form channels with Kv3.1-Kv3.2 heteromers that are kinetically distinct from one another and from MiRP/homomeric Kv3 channels. The findings illustrate a mechanism for dynamic expansion of the functional repertoire of Kv3.1 and Kv3.2 potassium currents and suggest roles for these α subunits outside the scope of sustained rapid neuronal firing.
    Original languageEnglish
    Pages (from-to)7884-7892
    Number of pages9
    JournalThe Journal of Biological Chemistry
    Volume279
    Issue number9
    DOIs
    Publication statusPublished - 2004

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