rdf:type |
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lifeskim:mentions |
|
pubmed:issue |
18
|
pubmed:dateCreated |
2001-9-21
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pubmed:abstractText |
The mitochondrial aspartate/glutamate carrier catalyzes an important step in both the urea cycle and the aspartate/malate NADH shuttle. Citrin and aralar1 are homologous proteins belonging to the mitochondrial carrier family with EF-hand Ca(2+)-binding motifs in their N-terminal domains. Both proteins and their C-terminal domains were overexpressed in Escherichia coli, reconstituted into liposomes and shown to catalyze the electrogenic exchange of aspartate for glutamate and a H(+). Overexpression of the carriers in transfected human cells increased the activity of the malate/aspartate NADH shuttle. These results demonstrate that citrin and aralar1 are isoforms of the hitherto unidentified aspartate/glutamate carrier and explain why mutations in citrin cause type II citrullinemia in humans. The activity of citrin and aralar1 as aspartate/glutamate exchangers was stimulated by Ca(2+) on the external side of the inner mitochondrial membrane, where the Ca(2+)-binding domains of these proteins are localized. These results show that the aspartate/glutamate carrier is regulated by Ca(2+) through a mechanism independent of Ca(2+) entry into mitochondria, and suggest a novel mechanism of Ca(2+) regulation of the aspartate/malate shuttle.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11566871-10369257,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11566871-10642534,
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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/Amino Acid Transport Systems, Acidic,
http://linkedlifedata.com/resource/pubmed/chemical/Antiporters,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Membrane Transport...,
http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Organic Anion Transporters,
http://linkedlifedata.com/resource/pubmed/chemical/Proteolipids,
http://linkedlifedata.com/resource/pubmed/chemical/SLC25A12 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/aspartate-glutamate carrier,
http://linkedlifedata.com/resource/pubmed/chemical/citrin,
http://linkedlifedata.com/resource/pubmed/chemical/proteoliposomes
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
|
pubmed:issn |
0261-4189
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pubmed:author |
pubmed-author:IijimaMM,
pubmed-author:KobayashiKK,
pubmed-author:LasorsaF MFM,
pubmed-author:PalmieriFF,
pubmed-author:PalmieriLL,
pubmed-author:PardoBB,
pubmed-author:RunswickM JMJ,
pubmed-author:SahekiTT,
pubmed-author:SatrústeguiJJ,
pubmed-author:WalkerJ EJE,
pubmed-author:del ArcoAA
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pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5060-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11566871-Humans,
pubmed-meshheading:11566871-Calcium,
pubmed-meshheading:11566871-Kinetics,
pubmed-meshheading:11566871-Escherichia coli,
pubmed-meshheading:11566871-Mitochondria,
pubmed-meshheading:11566871-Models, Chemical,
pubmed-meshheading:11566871-Membrane Transport Proteins,
pubmed-meshheading:11566871-Cell Line,
pubmed-meshheading:11566871-Proteolipids,
pubmed-meshheading:11566871-Carrier Proteins,
pubmed-meshheading:11566871-Mitochondrial Proteins
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