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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1995-2-9
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pubmed:abstractText |
The Saccharomyces cerevisiae protein SEC14p is required for Golgi function and cell viability in vivo. This requirement is obviated by mutations that specifically inactivate the CDP-choline pathway for phosphatidylcholine biosynthesis. The biochemical basis for the in vivo relationship between SEC14p function and the CDP-choline pathway has remained obscure. We now report that SEC14p effects an in vivo depression of CDP-choline pathway activity by inhibiting choline-phosphate cytidylyltransferase (CCTase; EC 2.7.7.15), the rate-determining enzyme of the CDP-choline pathway. Moreover, this SEC14p-mediated inhibition of CCTase was recapitulated in vitro and was saturable. Finally, whereas the SEC14p-dependent inhibition of CCTase in vitro was markedly reduced under assay conditions that were expected to increase levels of phosphatidylinositol-bound SEC14p, assay conditions expected to increase levels of phosphatidylcholine-bound SEC14p resulted in significant potentiation of CCTase inhibition. The collective data suggest that the phosphatidylcholine-bound form of SEC14p effects an essential repression of CDP-choline pathway activity in Golgi membranes by inhibiting CCTase and that the phospholipid-binding/exchange activity of SEC14p represents a mechanism by which the regulatory activity of SEC14p is itself controlled.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7816798-13366992,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7816798-14731807,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7816798-17246236,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7816798-1856213,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7816798-1883207,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7816798-1898771,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7816798-1997207,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7816798-2091833,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7816798-2215682,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7816798-2407740,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7816798-2466847,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7816798-2536698,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7816798-2777797,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7816798-2826147,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7816798-3029130,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7816798-3888957,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7816798-6299731,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7816798-6336730,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7816798-6996832,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7816798-7961445,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7816798-8223486,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7816798-8294512
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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/Carbon Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Choline,
http://linkedlifedata.com/resource/pubmed/chemical/Choline-Phosphate...,
http://linkedlifedata.com/resource/pubmed/chemical/Cytidine Diphosphate Choline,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleotidyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipid Transfer Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SEC24 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
92
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
112-6
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pubmed:dateRevised |
2010-9-13
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pubmed:meshHeading |
pubmed-meshheading:7816798-Carbon Radioisotopes,
pubmed-meshheading:7816798-Carrier Proteins,
pubmed-meshheading:7816798-Choline,
pubmed-meshheading:7816798-Choline-Phosphate Cytidylyltransferase,
pubmed-meshheading:7816798-Cloning, Molecular,
pubmed-meshheading:7816798-Cytidine Diphosphate Choline,
pubmed-meshheading:7816798-Cytosol,
pubmed-meshheading:7816798-Escherichia coli,
pubmed-meshheading:7816798-Genotype,
pubmed-meshheading:7816798-Golgi Apparatus,
pubmed-meshheading:7816798-Intracellular Membranes,
pubmed-meshheading:7816798-Kinetics,
pubmed-meshheading:7816798-Ligands,
pubmed-meshheading:7816798-Membrane Proteins,
pubmed-meshheading:7816798-Models, Biological,
pubmed-meshheading:7816798-Nucleotidyltransferases,
pubmed-meshheading:7816798-Phosphatidylinositols,
pubmed-meshheading:7816798-Phospholipid Transfer Proteins,
pubmed-meshheading:7816798-Phospholipids,
pubmed-meshheading:7816798-Recombinant Proteins,
pubmed-meshheading:7816798-Saccharomyces cerevisiae,
pubmed-meshheading:7816798-Saccharomyces cerevisiae Proteins
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pubmed:year |
1995
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pubmed:articleTitle |
The Saccharomyces cerevisiae phosphatidylinositol-transfer protein effects a ligand-dependent inhibition of choline-phosphate cytidylyltransferase activity.
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pubmed:affiliation |
Department of Cell Biology, University of Alabama, Birmingham 35294-0005.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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