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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2006-5-29
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pubmed:abstractText |
Phosphatidylinositol transfer proteins (PITPs) regulate the interface between lipid metabolism and specific steps in membrane trafficking through the secretory pathway in eukaryotes. Herein, we describe the cis-acting information that controls PITPbeta localization in mammalian cells. We demonstrate PITPbeta localizes predominantly to the trans-Golgi network (TGN) and that this localization is independent of the phospholipid-bound state of PITPbeta. Domain mapping analyses show the targeting information within PITPbeta consists of three short C-terminal specificity elements and a nonspecific membrane-binding element defined by a small motif consisting of adjacent tryptophan residues (the W(202)W(203) motif). Combination of the specificity elements with the W(202)W(203) motif is necessary and sufficient to generate an efficient TGN-targeting module. Finally, we demonstrate that PITPbeta association with the TGN is tolerant to a range of missense mutations at residue serine 262, we describe the TGN localization of a novel PITPbeta isoform with a naturally occurring S262Q polymorphism, and we find no other genetic or pharmacological evidence to support the concept that PITPbeta localization to the TGN is obligately regulated by conventional protein kinase C (PKC) or the Golgi-localized PKC isoforms delta or epsilon. These latter findings are at odds with a previous report that conventional PKC-mediated phosphorylation of residue Ser262 is required for PITPbeta targeting to Golgi membranes.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-10488334,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-10531358,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-10801835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-10848624,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-11104777,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-11294895,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-11454456,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-11907258,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-11953429,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-11980708,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-12788952,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-14962392,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-15024053,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-15052341,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-15723057,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-15728190,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-16455519,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-1997207,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-2187869,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-2215682,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-2466847,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-6336730,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-7566155,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-7568025,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-7654206,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-7877991,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-7961615,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-8223486,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-8255295,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-8599109,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-8692861,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-8806448,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-9139830,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-9461221,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-9553090,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16540520-9670016
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1059-1524
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2498-512
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16540520-Amino Acid Sequence,
pubmed-meshheading:16540520-Animals,
pubmed-meshheading:16540520-COS Cells,
pubmed-meshheading:16540520-Cell Line,
pubmed-meshheading:16540520-Cercopithecus aethiops,
pubmed-meshheading:16540520-Genes, Reporter,
pubmed-meshheading:16540520-Green Fluorescent Proteins,
pubmed-meshheading:16540520-Mice,
pubmed-meshheading:16540520-Molecular Sequence Data,
pubmed-meshheading:16540520-Phospholipid Transfer Proteins,
pubmed-meshheading:16540520-Protein Transport,
pubmed-meshheading:16540520-Transfection,
pubmed-meshheading:16540520-trans-Golgi Network
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pubmed:year |
2006
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pubmed:articleTitle |
Specific and nonspecific membrane-binding determinants cooperate in targeting phosphatidylinositol transfer protein beta-isoform to the mammalian trans-Golgi network.
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pubmed:affiliation |
Department of Cell and Developmental Biology, Lineberger Comprehensive Cancer Center, University of North Carolina School of Medicine, Chapel Hill, NC 27599-7090, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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