AKT2/3 subunits render guard cell K+ channels Ca2+ sensitive

被引:54
作者
Ivashikina, N [1 ]
Deeken, R [1 ]
Fischer, S [1 ]
Ache, P [1 ]
Hedrich, R [1 ]
机构
[1] Univ Wurzburg, Dept Mol Plant Physiol & Biophys, Bioctr, Julius Von Sachs Inst Biosci, D-97082 Wurzburg, Germany
关键词
Arabidopsis; guard cells; potassium channel; calcium sensitivity; AKT2/3;
D O I
10.1085/jgp.200409211
中图分类号
Q4 [生理学];
学科分类号
071003 ;
摘要
Inward-rectifying K+ channels serve as a major pathway for Ca2+-sensitive K+ influx into guard cells. Arabidopsis thaliana guard cell inward-rectifying K+ channels are assembled from multiple K+ channel subunits. Following the recent isolation and characterization of an akt2/3-1 knockout mutant, we examined whether the AKT2/3 subunit carries the Ca2+ sensitivity of the guard cell inward rectifier. Quantification of RT-PCR products showed that despite the absence of AKT2 transcripts in guard cells of the knockout plant, expression levels of the other K+ channel subunits (KAT1, KAT2, AKT1, and AtKC1) remained largely unaffected. Patch-clamp experiments with guard cell protoplasts from wild type and akt2/3-1 mutant, however, revealed pronounced differences in Ca2+ sensitivity of the K+ inward rectifier. Wild-type channels were blocked by extracellular Ca2+ in a concentration- and voltage-dependent manner. Akt2/3-1 mutants lacked the voltage-dependent Ca2+ block, characteristic for the K+ inward rectifier. To confirm the akt2/3-1 phenotype, two independent knockout mutants, akt2-1 and akt2::En-1 were tested, demonstrating that the loss of AKT2/3 indeed affects the Ca2+ dependence of guard cell inward rectifier. In contrast to AKT2 knockout plants, AKT1, AtKC1, and KAT1 loss-of-function mutants retained Ca2+ block of the guard cell inward rectifier. When expressed in HEK293 cells, AKT2 channel displayed a pronounced susceptibility toward extracellular Ca2+, while the dominant guard cell K+ channel KAT2 was Ca2+ insensitive. Thus, we conclude that the AKT2/3 subunit constitutes the Ca2+ sensitivity of the guard cell K+ uptake channel.
引用
收藏
页码:483 / 492
页数:10
相关论文
共 60 条
[41]   Signal transduction and ion channels in guard cells [J].
MacRobbie, EAC .
PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY OF LONDON SERIES B-BIOLOGICAL SCIENCES, 1998, 353 (1374) :1475-1488
[42]   EFFECTS OF LIGHT DARK ON CATION FLUXES IN GUARD-CELLS OF COMMELINA-COMMUNIS L [J].
MACROBBIE, EAC .
JOURNAL OF EXPERIMENTAL BOTANY, 1983, 34 (149) :1695-1710
[43]   AKT3, a phloem-localized K+ channel, is blocked by protons [J].
Marten, I ;
Hoth, S ;
Deeken, R ;
Ache, P ;
Ketchum, KA ;
Hoshi, T ;
Hedrich, R .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (13) :7581-7586
[44]   Pollen tube development and competitive ability are impaired by disruption of a Shaker K+ channel in Arabidopsis [J].
Mouline, K ;
Véry, AA ;
Gaymard, F ;
Boucherez, J ;
Pilot, G ;
Devic, M ;
Bouchez, D ;
Thibaud, JB ;
Sentenac, H .
GENES & DEVELOPMENT, 2002, 16 (03) :339-350
[45]   Arabidopsis OST1 protein kinase mediates the regulation of stomatal aperture by abscisic acid and acts upstream of reactive oxygen species production [J].
Mustilli, AC ;
Merlot, S ;
Vavasseur, A ;
Fenzi, F ;
Giraudat, J .
PLANT CELL, 2002, 14 (12) :3089-3099
[46]   EXPRESSION OF AN ARABIDOPSIS POTASSIUM CHANNEL GENE IN GUARD-CELLS [J].
NAKAMURA, RL ;
MCKENDREE, WL ;
HIRSCH, RE ;
SEDBROOK, JC ;
GABER, RF ;
SUSSMAN, MR .
PLANT PHYSIOLOGY, 1995, 109 (02) :371-374
[47]  
NEHER E, 1992, METHOD ENZYMOL, V207, P123
[48]   A novel K+ channel expressed in carrot roots with a low susceptibility toward metal ions [J].
Paganetto, A ;
Bregante, M ;
Downey, P ;
Lo Schiavo, F ;
Hoth, S ;
Hedrich, R ;
Gambale, F .
JOURNAL OF BIOENERGETICS AND BIOMEMBRANES, 2001, 33 (01) :63-71
[49]   Auxin activates KAT1 and KAT2, two K+-channel genes expressed in seedlings of Arabidopsis thaliana [J].
Philippar, K ;
Ivashikina, N ;
Ache, P ;
Christian, M ;
Lüthen, H ;
Palme, K ;
Hedrich, R .
PLANT JOURNAL, 2004, 37 (06) :815-827
[50]   Guard cell inward K+ channel activity in Arabidopsis involves expression of the twin channel subunits KAT1 and KAT2 [J].
Pilot, G ;
Lacombe, B ;
Gaymard, F ;
Chérel, I ;
Boucherez, J ;
Thibaud, JB ;
Sentenac, H .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (05) :3215-3221