TY  - JOUR
A1  - Sato, A
A1  - Gambale, Franco
A1  - Dreyer, Ingo
A1  - Uozumi, N
T1  - Posttranslational inodification affects K+ current of plant K+ channel
Y1  - 2006
ER  - 
TY  - JOUR
A1  - Voelker, Camilla
A1  - Gomez-Porras, Judith Lucia
A1  - Becker, Dirk
A1  - Hamamoto, Shin
A1  - Uozumi, Nobuyuki
A1  - Gambale, Franco
A1  - Müller-Röber, Bernd
A1  - Czempinski, Katrin
A1  - Dreyer, Ingo
T1  - Roles of tandem-pore K plus channels in plants : a puzzle still to be solved
N2  - The group of voltage-independent K+ channels in Arabidopsis thaliana consists of six members, five tandem-pore channels (TPK1-TPK5) and a single K-ir-like channel (KCO3). All TPK/KCO channels are located at the vacuolar membrane except for TPK4, which was shown to be a plasma membrane channel in pollen. The vacuolar channels interact with 14-3-3 proteins (also called General Regulating Factors, GRFs), indicating regulation at the level of protein-protein interactions. Here we review current knowledge about these ion channels and their genes, and highlight open questions that need to be urgently addressed in future studies to fully appreciate the physiological functions of these ion channels.
Y1  - 2010
UR  - http://www3.interscience.wiley.com/cgi-bin/issn?DESCRIPTOR=PRINTISSN&VALUE=1435-8603
U6  - https://doi.org/10.1111/j.1438-8677.2010.00353.x
SN  - 1435-8603
ER  - 
TY  - JOUR
A1  - Naso, Alessia
A1  - Dreyer, Ingo
A1  - Pedemonte, Laura
A1  - Testa, Ilaria
A1  - Gomez-Porras, Judith Lucia
A1  - Usai, Cesare
A1  - Müller-Röber, Bernd
A1  - Diaspro, Alberto
A1  - Gambale, Franco
A1  - Picco, Cristiana
T1  - The role of the C-terminus for functional heteromerization of the plant channel KDC1
N2  - Voltage-gated potassium channels are formed by the assembly of four identical (homotetramer) or different (heterotetramer) subunits. Tetramerization of plant potassium channels involves the C-terminus of the protein. We investigated the role of the C-terminus of KDC1, a Shaker-like inward-rectifying K+ channel that does not form functional homomeric channels, but participates in the formation of heteromeric complexes with other potassium alpha- subunits when expressed in Xenopus oocytes. The interaction of KDC1 with KAT1 was investigated using the yeast two- hybrid system, fluorescence and electrophysiological studies. We found that the KDC1-EGFP fusion protein is not targeted to the plasma membrane of Xenopus oocytes unless it is coexpressed with KAT1. Deletion mutants revealed that the KDC1 C- terminus is involved in heteromerization. Two domains of the C-terminus, the region downstream the putative cyclic nucleotide binding domain and the distal part of the C-terminus called K-HA domain, contributed to a different extent to channel assembly. Whereas the first interacting region of the C-terminus was necessary for channel heteromerization, the removal of the distal KHA domain decreased but did not abolish the formation of heteromeric complexes. Similar results were obtained when coexpressing KDC1 with the KAT1-homolog KDC2 from carrots, thus indicating the physiological significance of the KAT1/KDC1 characterization. Electrophysiological experiments showed furthermore that the heteromerization capacity of KDC1 was negatively influenced by the presence of the enhanced green fluorescence protein fusion.
Y1  - 2009
UR  - http://www.sciencedirect.com/science/journal/00063495
U6  - https://doi.org/10.1016/j.bpj.2009.02.055
SN  - 0006-3495
ER  -