TY  - JOUR
A1  - Gajdanowicz, Pawel
A1  - Garcia-Mata, Carlos
A1  - Gonzalez, Wendy
A1  - Morales-Navarro, Samuel Elïas
A1  - Sharma, Tripti
A1  - Gonzalez-Nilo, Fernando Danilo
A1  - Gutowicz, Jan
A1  - Müller-Röber, Bernd
A1  - Blatt, Michael R.
A1  - Dreyer, Ingo
T1  - Distinct roles of the last transmembrane domain in controlling Arabidopsis K+ channel activity
N2  - 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 Kin 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 Kin 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.
Y1  - 2009
UR  - http://www3.interscience.wiley.com/cgi-bin/issn?DESCRIPTOR=PRINTISSN&VALUE=0028-646X
U6  - https://doi.org/10.1111/j.1469-8137.2008.02749.x
SN  - 0028-646X
ER  -