Source:http://linkedlifedata.com/resource/pubmed/id/14960315
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-3
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pubmed:dateCreated |
2004-2-12
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pubmed:abstractText |
Precise regulation of calcium transporters is essential for modulating the Ca2+ signaling network that is involved in the growth and adaptation of all organisms. The Arabidopsis H+/Ca2+ antiporter, CAX1, is a high capacity and low affinity Ca2+ transporter and several CAX1-like transporters are found in Arabidopsis. When heterologously expressed in yeast, CAX1 is unable to suppress the Ca2+ hypersensitivity of yeast vacuolar Ca2+ transporter mutants due to an N-terminal autoinhibition mechanism that prevents Ca2+ transport. Using a yeast screen, we have identified CAX nteracting Protein 4 (CXIP4) that activated full-length CAX1, but not full-length CAX2, CAX3 or CAX4. CXIP4 encodes a novel plant protein with no bacterial, fungal, animal, or mammalian homologs. Expression of a GFP-CXIP4 fusion in yeast and plant cells suggests that CXIP4 is targeted predominantly to the nucleus. Using a yeast growth assay, CXIP4 activated a chimeric CAX construct that contained specific portions of the N-terminus of CAX1. Together with other recent studies, these results suggest that CAX1 is regulated by several signaling molecules that converge on the N-terminus of CAX1 to regulate H+/Ca2+ antiport.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
559
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
99-106
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:14960315-Amino Acid Sequence,
pubmed-meshheading:14960315-Arabidopsis Proteins,
pubmed-meshheading:14960315-Carrier Proteins,
pubmed-meshheading:14960315-Cell Nucleus,
pubmed-meshheading:14960315-Green Fluorescent Proteins,
pubmed-meshheading:14960315-Luminescent Proteins,
pubmed-meshheading:14960315-Nuclear Proteins,
pubmed-meshheading:14960315-Plant Leaves,
pubmed-meshheading:14960315-Recombinant Fusion Proteins,
pubmed-meshheading:14960315-Sequence Alignment,
pubmed-meshheading:14960315-Tobacco,
pubmed-meshheading:14960315-Yeasts
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pubmed:year |
2004
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pubmed:articleTitle |
Characterization of CXIP4, a novel Arabidopsis protein that activates the H+/Ca2+ antiporter, CAX1.
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pubmed:affiliation |
United States Department of Agriculture/Agricultural Research Service Children's Nutrition Research Center, Baylor College of Medicine, 1100 Bates Street, Houston, TX 77030, USA. ncheng@bcm.tmc.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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