Complex interactions among residues within pore region determine the K+ dependence of a KAT1-type potassium channel AmKAT1

Plant J. 2015 Aug;83(3):401-12. doi: 10.1111/tpj.12891. Epub 2015 Jun 27.

Abstract

KAT1-type channels mediate K(+) influx into guard cells that enables stomatal opening. In this study, a KAT1-type channel AmKAT1 was cloned from the xerophyte Ammopiptanthus mongolicus. In contrast to most KAT1-type channels, its activation is strongly dependent on external K(+) concentration, so it can be used as a model to explore the mechanism for the K(+) -dependent gating of KAT1-type channels. Domain swapping between AmKAT1 and KAT1 reveals that the S5-pore-S6 region controls the K(+) dependence of AmKAT1, and residue substitutions show that multiple residues within the S5-Pore linker and Pore are involved in its K(+) -dependent gating. Importantly, complex interactions occur among these residues, and it is these interactions that determine its K(+) dependence. Finally, we analyzed the potential mechanism for the K(+) dependence of AmKAT1, which could originate from the requirement of K(+) occupancy in the selectivity filter to maintain its conductive conformation. These results provide new insights into the molecular basis of the K(+) -dependent gating of KAT1-type channels.

Keywords: Ammopiptanthus mongolicus; K+-dependent gating; KAT1-type channel; potassium channel; protein-cation interaction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis Proteins / physiology*
  • Ion Channel Gating / genetics*
  • Ion Channel Gating / physiology
  • Plant Stomata / physiology*
  • Potassium Channels / physiology*
  • Potassium Channels, Inwardly Rectifying / physiology*

Substances

  • Arabidopsis Proteins
  • KAT1 protein, Arabidopsis
  • Potassium Channels
  • Potassium Channels, Inwardly Rectifying