rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
3
|
pubmed:dateCreated |
2005-4-21
|
pubmed:databankReference |
|
pubmed:abstractText |
A prominent regulatory property of plant shaker-type K+ channels is the 'rundown' that causes channel closure upon membrane excision from the cell, implicating intracellular factor(s) in maintaining channel activity. One such factor has been identified as hydrolysable ATP-Mg although the mechanism for ATP function remains unknown. Here we report identification of phosphatidylinositol (PI) phosphates (PIPs) as essential regulators for the voltage-dependent and -independent activation of plant shaker-type channels such as SKOR, an outward rectifying K+ channel. Inhibition of PI kinase activity abolished the function of ATP-Mg in restoration of rundown channel activity, demonstrating that PIPs production by PI kinases and ATP-Mg underlies ATP-induced activation of the rundown channel. We also identified aluminum block as a common feature of the plant shaker-type channels and provided evidence that aluminum block of these channels may result from Al interaction with PIPs.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aluminum,
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/KAT1 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels, Inwardly...,
http://linkedlifedata.com/resource/pubmed/chemical/SKOR protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Shaker Superfamily of Potassium...
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0960-7412
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
42
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
433-43
|
pubmed:dateRevised |
2006-11-7
|
pubmed:meshHeading |
pubmed-meshheading:15842627-Aluminum,
pubmed-meshheading:15842627-Animals,
pubmed-meshheading:15842627-Arabidopsis,
pubmed-meshheading:15842627-Arabidopsis Proteins,
pubmed-meshheading:15842627-Ion Channel Gating,
pubmed-meshheading:15842627-Membrane Potentials,
pubmed-meshheading:15842627-Molecular Sequence Data,
pubmed-meshheading:15842627-Oocytes,
pubmed-meshheading:15842627-Organisms, Genetically Modified,
pubmed-meshheading:15842627-Phosphatidylinositol Phosphates,
pubmed-meshheading:15842627-Potassium Channels,
pubmed-meshheading:15842627-Potassium Channels, Inwardly Rectifying,
pubmed-meshheading:15842627-Shaker Superfamily of Potassium Channels,
pubmed-meshheading:15842627-Signal Transduction,
pubmed-meshheading:15842627-Xenopus laevis
|
pubmed:year |
2005
|
pubmed:articleTitle |
An essential function of phosphatidylinositol phosphates in activation of plant shaker-type K+ channels.
|
pubmed:affiliation |
Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720, USA.
|
pubmed:publicationType |
Journal Article
|