Complex interactions among residues within pore region determine the K+ dependence of a KAT1‐type potassium channel AmKAT1 |
| |
Authors: | Guangzhe Yang Hervé Sentenac Anne‐Aliénor Véry Yanhua Su |
| |
Institution: | 1. State Key Laboratory of Soil and Sustainable Agriculture, Institute of Soil Science, Chinese Academy of Sciences, Nanjing, China;2. Biochimie & Physiologie Moléculaire des Plantes, UMR 5004 CNRS/386 INRA/SupAgro Montpellier/Université Montpellier 2, Montpellier Cedex 2, France |
| |
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 |
|
|