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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2003-12-18
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pubmed:abstractText |
Glyceraldehyde-3-phosphate dehydrogenases catalyze key steps in energy and reducing power partitioning in cells of higher plants. Phosphorylated non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) present in heterotrophic cells of wheat (Triticum aestivum) was activated up to 3-fold by MgCl2. The effect was not observed with the non-phosphorylated enzyme found in leaves. The divalent cation also affected the response of the enzyme from endosperm and shoots to adenine nucleotides and inorganic pyrophosphate. Gel filtration chromatography, co-immunoprecipitation followed by immunostaining, and the use of a phosphopeptide containing a canonical binding motif showed that MgCl2 actually disrupted the interaction between GAPN and a 14-3-3 regulatory protein. After interaction with 14-3-3, phosphorylated GAPN exhibits a 3-fold lower Vmax and higher sensitivity to inhibition by ATP and pyrophosphate. Results suggest that GAPN is a target for regulation by phosphorylation, levels of divalent cations, and 14-3-3 proteins. The regulatory mechanism could be critical to maintain levels of energy and reductants in the cytoplasm of heterotrophic plant cells.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-10341439,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-10634907,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-10859205,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-109446,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-11019808,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-11150658,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-11351068,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-11553742,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-12196098,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-12387887,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-12508070,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-12516872,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-12853467,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-220918,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-3070872,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-3341766,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-8096814,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-8205002,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-8215424,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-9398266,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-942051,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-9461340,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-9516476,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14681537-9871366
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/14-3-3 Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Monophosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Divalent,
http://linkedlifedata.com/resource/pubmed/chemical/Diphosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Glyceraldehyde-3-Phosphate...,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine 3-Monooxygenase
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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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 |
133
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2081-8
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pubmed:dateRevised |
2010-9-21
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pubmed:meshHeading |
pubmed-meshheading:14681537-14-3-3 Proteins,
pubmed-meshheading:14681537-Adenosine Diphosphate,
pubmed-meshheading:14681537-Adenosine Monophosphate,
pubmed-meshheading:14681537-Adenosine Triphosphate,
pubmed-meshheading:14681537-Cations, Divalent,
pubmed-meshheading:14681537-Cells, Cultured,
pubmed-meshheading:14681537-Chromatography, Gel,
pubmed-meshheading:14681537-Diphosphates,
pubmed-meshheading:14681537-Glyceraldehyde-3-Phosphate Dehydrogenases,
pubmed-meshheading:14681537-Kinetics,
pubmed-meshheading:14681537-Phosphoproteins,
pubmed-meshheading:14681537-Phosphorylation,
pubmed-meshheading:14681537-Plant Proteins,
pubmed-meshheading:14681537-Triticum,
pubmed-meshheading:14681537-Tyrosine 3-Monooxygenase
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pubmed:year |
2003
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pubmed:articleTitle |
Phosphorylated non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from heterotrophic cells of wheat interacts with 14-3-3 proteins.
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pubmed:affiliation |
Instituto Tecnológico de Chascomús, Camino Circunvalación Laguna km 6, CC 164, B7130IWA Chascomús, Argentina.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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