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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2001-11-13
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pubmed:abstractText |
Regulation of Ca(2+) transport determines the duration of a Ca(2+) signal, and hence, the nature of the biological response. Ca(2+)/H+ antiporters such as CAX1 (cation exchanger 1), play a key role in determining cytosolic Ca(2+) levels. Analysis of a full-length CAX1 clone suggested that the CAX1 open reading frame contains an additional 36 amino acids at the N terminus that were not found in the original clone identified by suppression of yeast (Saccharomyces cerevisiae) vacuolar Ca(2+) transport mutants. The long CAX1 (lCAX1) could not suppress the yeast Ca(2+) transport defects despite localization to the yeast vacuole. Calmodulin could not stimulate lCAX1 Ca(2+)/H+ transport in yeast; however, minor alterations in the 36-amino acid region restored Ca(2+)/H+ transport. Sequence analysis suggests that a 36-amino acid N-terminal regulatory domain may be present in all Arabidopsis CAX-like genes. Together, these results suggest a structural feature involved in regulation of Ca(2+)/H+ antiport.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11706183-10336626,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11706183-10559438,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11706183-10600390,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/11706183-10823962,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/11706183-10948258,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/11706183-9990037
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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 |
Nov
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pubmed:issn |
0032-0889
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
127
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1020-9
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pubmed:dateRevised |
2010-9-14
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pubmed:meshHeading |
pubmed-meshheading:11706183-Amino Acid Sequence,
pubmed-meshheading:11706183-Antiporters,
pubmed-meshheading:11706183-Arabidopsis,
pubmed-meshheading:11706183-Arabidopsis Proteins,
pubmed-meshheading:11706183-Calcium,
pubmed-meshheading:11706183-Calcium-Binding Proteins,
pubmed-meshheading:11706183-Cation Transport Proteins,
pubmed-meshheading:11706183-Chromosome Mapping,
pubmed-meshheading:11706183-Cytosol,
pubmed-meshheading:11706183-Hydrogen,
pubmed-meshheading:11706183-Hydrogen-Ion Concentration,
pubmed-meshheading:11706183-Ion Transport,
pubmed-meshheading:11706183-Molecular Sequence Data,
pubmed-meshheading:11706183-Protein Structure, Tertiary,
pubmed-meshheading:11706183-Saccharomyces cerevisiae,
pubmed-meshheading:11706183-Sequence Homology, Amino Acid,
pubmed-meshheading:11706183-Signal Transduction,
pubmed-meshheading:11706183-Vacuoles
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pubmed:year |
2001
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pubmed:articleTitle |
Regulation of CAX1, an Arabidopsis Ca(2+)/H+ antiporter. Identification of an N-terminal autoinhibitory domain.
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pubmed:affiliation |
Plant Physiology Group, U.S. Department of Agriculture/Agricultural Research Service, Baylor College of Medicine, 1100 Bates Street, Houston, TX 77030, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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