TY - JOUR
T1 - Cyclic adenosine monophosphate regulates calcium channels in the plasma membrane of Arabidopsis leaf guard and mesophyll cells
AU - Lemtiri-Chlieh, Fouad
AU - Berkowitz, Gerald A.
PY - 2004/8/20
Y1 - 2004/8/20
N2 - The effect of cAMP on Ca2+-permeable channels from Arabidopsis thaliana leaf guard cell and mesophyll cell protoplasts was studied using the patch clamp technique. In the whole cell configuration, dibutyryl cAMP was found to increase a hyperpolarization-activated Ba2+ conductance (I Ba). The increase of IBa was blocked by the addition of GdCl3. In excised outside-out patches, the addition of dibutyryl cAMP consistently activated a channel with particularly fast gating kinetics. Current/voltage analyses indicated a single channel conductance of ∼13 picosiemens. In patches where we measured some channel activity prior to cAMP application, the data suggest that cAMP enhances channel activity without affecting the single channel conductance. The cAMP activation of these channels was reversible upon washout. The results obtained with excised patches indicate that the cAMP-activated IBa seen in the whole cell configuration could be explained by a direct effect of cAMP on the Ca2+ channel itself or a close entity to the channel. This work represents the first demonstration using patch clamp analysis of the presence in plant cell membranes of an ion channel directly activated by cAMP.
AB - The effect of cAMP on Ca2+-permeable channels from Arabidopsis thaliana leaf guard cell and mesophyll cell protoplasts was studied using the patch clamp technique. In the whole cell configuration, dibutyryl cAMP was found to increase a hyperpolarization-activated Ba2+ conductance (I Ba). The increase of IBa was blocked by the addition of GdCl3. In excised outside-out patches, the addition of dibutyryl cAMP consistently activated a channel with particularly fast gating kinetics. Current/voltage analyses indicated a single channel conductance of ∼13 picosiemens. In patches where we measured some channel activity prior to cAMP application, the data suggest that cAMP enhances channel activity without affecting the single channel conductance. The cAMP activation of these channels was reversible upon washout. The results obtained with excised patches indicate that the cAMP-activated IBa seen in the whole cell configuration could be explained by a direct effect of cAMP on the Ca2+ channel itself or a close entity to the channel. This work represents the first demonstration using patch clamp analysis of the presence in plant cell membranes of an ion channel directly activated by cAMP.
UR - http://www.scopus.com/inward/record.url?scp=4143112372&partnerID=8YFLogxK
U2 - 10.1074/jbc.M400311200
DO - 10.1074/jbc.M400311200
M3 - Article
C2 - 15199067
AN - SCOPUS:4143112372
SN - 0021-9258
VL - 279
SP - 35306
EP - 35312
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 34
ER -