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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
23
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pubmed:dateCreated |
1997-1-27
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pubmed:abstractText |
Calcium-Dependent Protein Kinases (CDPKs) in higher plants contain a C-terminal calmodulin-like regulatory domain. Little is known regarding physiological CDPK targets. Both kinase activity and multiple Ca2+-dependent signaling pathways have been implicated in the control of stomatal guard cell movements. To determine whether CDPK or other protein kinases could have a role in guard cell signaling, purified and recombinant kinases were applied to Vicia faba guard cell vacuoles during patch-clamp experiments. CDPK activated novel vacuolar chloride (VCL) and malate conductances in guard cells. Activation was dependent on both Ca2+ and ATP. Furthermore, VCL activation occurred in the absence of Ca2+ using a Ca2+-independent, constitutively active, CDPK* mutant. Protein kinase A showed weaker activation (22% as compared with CDPK). Current reversals in whole vacuole recordings shifted with the Nernst potential for Cl-and vanished in glutamate. Single channel recordings showed a CDPK-activated 34 +/- 5 pS Cl- channel. VCL channels were activated at physiological potentials enabling Cl- uptake into vacuoles. VCL channels may provide a previously unidentified, but necessary, pathway for anion uptake into vacuoles required for stomatal opening. CDPK-activated VCL currents were also observed in red beet vacuoles suggesting that these channels may provide a more general mechanism for kinase-dependent anion uptake.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-11540065,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-11607281,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-11607582,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-1279437,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-1373227,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-1400282,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-1528115,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-16653096,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-16653198,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-16657817,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-16664518,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-16665276,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-16665348,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-16667955,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-16669053,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-1763075,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-1852075,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-1912486,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-2174559,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-2388697,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-6270629,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-722275,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-7514272,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-7519678,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-7539989,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-7592955,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-7610156,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-7678414,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-7916621,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-8003490,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-8003491,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-8117660,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-8325505,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-8440720,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-8620541,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-8754686,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8978683-8756605
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pubmed:keyword |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6564-74
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pubmed:dateRevised |
2010-9-13
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pubmed:meshHeading |
pubmed-meshheading:8978683-Adenosine Triphosphate,
pubmed-meshheading:8978683-Calcium,
pubmed-meshheading:8978683-Cell Movement,
pubmed-meshheading:8978683-Chloride Channels,
pubmed-meshheading:8978683-Cytosol,
pubmed-meshheading:8978683-Fabaceae,
pubmed-meshheading:8978683-Kinetics,
pubmed-meshheading:8978683-Membrane Potentials,
pubmed-meshheading:8978683-Patch-Clamp Techniques,
pubmed-meshheading:8978683-Plants, Medicinal,
pubmed-meshheading:8978683-Protein-Serine-Threonine Kinases,
pubmed-meshheading:8978683-Species Specificity,
pubmed-meshheading:8978683-Vacuoles,
pubmed-meshheading:8978683-Vegetables
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pubmed:year |
1996
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pubmed:articleTitle |
A novel chloride channel in Vicia faba guard cell vacuoles activated by the serine/threonine kinase, CDPK.
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pubmed:affiliation |
Department of Biology and Center for Molecular Genetics, University of California, San Diego, La Jolla 92093-0116, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, Non-P.H.S.
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