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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1999-3-3
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pubmed:databankReference |
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pubmed:abstractText |
The assembly of triglyceride-rich lipoproteins requires the formation in the endoplasmic reticulum of a complex between apolipoprotein B (apoB), a microsomal triglyceride transfer protein (MTP), and protein disulfide isomerase (PDI). In the MTP complex, the amino-terminal region of MTP (residues 22-303) interacts with the amino-terminal region of apoB (residues 1-264). Here, we report the identification and characterization of a site on apoB between residues 512 and 721, which interacts with residues 517-603 of MTP. PDI binds in close proximity to this apoB binding site on MTP. The proximity of these binding sites on MTP for PDI and amino acids 512-721 of apoB was evident from studies carried out in a yeast two-hybrid system and by co-immunoprecipitation. The expression of PDI with MTP and apoB16 (residues 1-721) in the baculovirus expression system reduced the amount of MTP co-immunoprecipitated with apoB by 73%. The interaction of residues 512-721 of apoB with MTP facilitates lipoprotein production. Mutations of apoB that markedly reduced this interaction also reduced the level of apoB-containing lipoprotein secretion.
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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 |
Jan
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pubmed:issn |
0021-9258
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pubmed:author |
pubmed-author:AmeyJJ,
pubmed-author:AndersonT ATA,
pubmed-author:BanaszakL JLJ,
pubmed-author:BradburyPP,
pubmed-author:ChesterS ASA,
pubmed-author:HancockJ MJM,
pubmed-author:HarrisonG BGB,
pubmed-author:KöchlSS,
pubmed-author:LevittD GDG,
pubmed-author:MannC JCJ,
pubmed-author:RitchieP JPJ,
pubmed-author:ScottJJ,
pubmed-author:ShouldersC CCC
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3159-64
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:9915855-Amino Acid Sequence,
pubmed-meshheading:9915855-Animals,
pubmed-meshheading:9915855-Apolipoproteins B,
pubmed-meshheading:9915855-Binding Sites,
pubmed-meshheading:9915855-Caenorhabditis elegans,
pubmed-meshheading:9915855-Carrier Proteins,
pubmed-meshheading:9915855-Drosophila melanogaster,
pubmed-meshheading:9915855-Humans,
pubmed-meshheading:9915855-Lampreys,
pubmed-meshheading:9915855-Microsomes,
pubmed-meshheading:9915855-Models, Molecular,
pubmed-meshheading:9915855-Molecular Sequence Data,
pubmed-meshheading:9915855-Protein Binding,
pubmed-meshheading:9915855-Protein Disulfide-Isomerases,
pubmed-meshheading:9915855-Sequence Alignment,
pubmed-meshheading:9915855-Xenopus laevis
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pubmed:year |
1999
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pubmed:articleTitle |
A common binding site on the microsomal triglyceride transfer protein for apolipoprotein B and protein disulfide isomerase.
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pubmed:affiliation |
Medical Research Council Molecular Medicine Group, Imperial College School of Medicine, Hammersmith Hospital, London W12 0NN, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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