Distinct domains of the voltage-gated K+ channel Kvβ1.3 β-subunit affect voltage-dependent gating

Victor N. Uebele, Sarah K. England, Daniel J. Gallagher, Dirk J. Snyders, Paul B. Bennett, Michael M. Tamkun

Research output: Contribution to journalArticlepeer-review

49 Scopus citations

Abstract

The Kvβ1.3 subunit confers a voltage-dependent, partial inactivation (time constant = 5.76 ± 0.14 ms at +50 mV), an enhanced slow inactivation, a hyperpolarizing shift in the activation midpoint, and an increase in the deactivation time constant of the Kv1.5 delayed rectifier. Removal of the first 10 amino acids from Kvβ1.3 eliminated the effects on fast and slow inactivation but not the voltage shift in activation. Addition of the first 87 amino acids of Kvβ1.3 to the amino terminus of Kv1.5 reconstituted fast and slow inactivation without altering the midpoint of activation. Although an internal pore mutation that alters quinidine block (V512A) did not affect Kvβ1.3-mediated inactivation, a mutation of the external mouth of the pore (R485Y) increased the extent of fast inactivation while preventing the enhancement of slow inactivation. These data suggest that 1) Kvβ1.3-mediated effects involve at least two distinct domains of this β-subunit, 2) inactivation involves open channel block that is allosterically linked to the external pore, and 3) the Kvβ1.3-induced shift in the activation midpoint is functionally distinct from inactivation.

Original languageEnglish
Pages (from-to)C1485-C1495
JournalAmerican Journal of Physiology - Cell Physiology
Volume274
Issue number6 43-6
DOIs
StatePublished - Jun 1998

Keywords

  • C-type inactivation
  • N-type inactivation
  • Shaker-like potassium channel

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