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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
39
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pubmed:dateCreated |
2007-9-26
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pubmed:abstractText |
The Saccharomyces cerevisiae phosphatidylcholine/phosphatidylinositol transfer protein Sec14p is required for Golgi apparatus-derived vesicular transport through coordinate regulation of phospholipid metabolism. Sec14p is normally essential. The essential requirement for SEC14 can be bypassed by inactivation of (i) the CDP-choline pathway for phosphatidylcholine synthesis or (ii) KES1, which encodes an oxysterol binding protein. A unique screen was used to determine genome-wide genetic interactions for the essential gene SEC14 and to assess whether the two modes of "sec14 bypass" were similar or distinct. The results indicate that inactivation of the CDP-choline pathway allows cells with inactivated SEC14 to live through a mechanism distinct from that of inactivation of KES1. We go on to demonstrate an important biological function of Kes1p. Kes1p regulates Golgi apparatus-derived vesicular transport by inhibiting the function of Pik1p-generated Golgi apparatus phosphatidylinositol-4-phosphate (PI-4P). Kes1p affects both the availability and level of Golgi apparatus PI-4P. A set of potential PI-4P-responsive proteins that include the Rab GTPase Ypt31p and its GTP exchange factor are described.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-10397762,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-10567405,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-10587649,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-10930462,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-11102533,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-11743205,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-11854411,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-11916983,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-14562106,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-15173322,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-15271978,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-15574876,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-15617515,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-15723057,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-15893935,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-16018544,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-16096648,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-16136145,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-16155567,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-16269340,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-16365163,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-16585271,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-17041589,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-17220896,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-1997207,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-2466847,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-8182083,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-8978672,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17881569-8978673
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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/1-Phosphatidylinositol 4-Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/KES1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PIK1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylcholines,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipid Transfer Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Steroid,
http://linkedlifedata.com/resource/pubmed/chemical/SEC14 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sterols,
http://linkedlifedata.com/resource/pubmed/chemical/YPT31 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Fructofuranosidase,
http://linkedlifedata.com/resource/pubmed/chemical/phosphatidylinositol 4-phosphate,
http://linkedlifedata.com/resource/pubmed/chemical/rab GTP-Binding Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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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 |
25
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pubmed:volume |
104
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15352-7
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:17881569-1-Phosphatidylinositol 4-Kinase,
pubmed-meshheading:17881569-Genome, Fungal,
pubmed-meshheading:17881569-Golgi Apparatus,
pubmed-meshheading:17881569-Membrane Proteins,
pubmed-meshheading:17881569-Models, Biological,
pubmed-meshheading:17881569-Phosphatidylcholines,
pubmed-meshheading:17881569-Phosphatidylinositol Phosphates,
pubmed-meshheading:17881569-Phosphatidylinositols,
pubmed-meshheading:17881569-Phospholipid Transfer Proteins,
pubmed-meshheading:17881569-Receptors, Steroid,
pubmed-meshheading:17881569-Saccharomyces cerevisiae,
pubmed-meshheading:17881569-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:17881569-Sterols,
pubmed-meshheading:17881569-beta-Fructofuranosidase,
pubmed-meshheading:17881569-rab GTP-Binding Proteins
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pubmed:year |
2007
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pubmed:articleTitle |
The oxysterol binding protein Kes1p regulates Golgi apparatus phosphatidylinositol-4-phosphate function.
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pubmed:affiliation |
Department of Pediatrics, Dalhousie University, Halifax, NS, Canada B3H 4H7.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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