Distinct roles of the last transmembrane domain in controlling Arabidopsis K+ channel activity

The family of voltage-gated potassium channels in plants presumably evolved from a common ancestor and includes both inward-rectifying (K(in)) channels that allow plant cells to accumulate K(+) and outward-rectifying (K(out)) channels that mediate K(+) efflux. Despite their close structural similari...

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Veröffentlicht in:The New phytologist. - 1979. - 182(2009), 2 vom: 01., Seite 380-391
1. Verfasser: Gajdanowicz, Pawel (VerfasserIn)
Weitere Verfasser: Garcia-Mata, Carlos, Gonzalez, Wendy, Morales-Navarro, Samuel Elías, Sharma, Tripti, González-Nilo, Fernando Danilo, Gutowicz, Jan, Mueller-Roeber, Bernd, Blatt, Michael R, Dreyer, Ingo
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2009
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Arabidopsis Proteins KAT1 protein, Arabidopsis Potassium Channels, Inwardly Rectifying Potassium Channels, Voltage-Gated SKOR protein, Arabidopsis Shaker Superfamily of Potassium Channels
Beschreibung
Zusammenfassung:The family of voltage-gated potassium channels in plants presumably evolved from a common ancestor and includes both inward-rectifying (K(in)) channels that allow plant cells to accumulate K(+) and outward-rectifying (K(out)) channels that mediate K(+) efflux. Despite their close structural similarities, the activity of K(in) channels is largely independent of K(+) and depends only on the transmembrane voltage, whereas that of K(out) channels responds to the membrane voltage and the prevailing extracellular K(+) concentration. Gating of potassium channels is achieved by structural rearrangements within the last transmembrane domain (S6). Here we investigated the functional equivalence of the S6 helices of the K(in) channel KAT1 and the K(out) channel SKOR by domain-swapping and site-directed mutagenesis. Channel mutants and chimeras were analyzed after expression in Xenopus oocytes. We identified two discrete regions that influence gating differently in both channels, demonstrating a lack of functional complementarity between KAT1 and SKOR. Our findings are supported by molecular models of KAT1 and SKOR in the open and closed states. The role of the S6 segment in gating evolved differently during specialization of the two channel subclasses, posing an obstacle for the transfer of the K(+)-sensor from K(out) to K(in) channels
Beschreibung:Date Completed 17.07.2009
Date Revised 20.10.2021
published: Print-Electronic
Citation Status MEDLINE
ISSN:1469-8137
DOI:10.1111/j.1469-8137.2008.02749.x