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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 1
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pubmed:dateCreated |
2003-12-15
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pubmed:abstractText |
ApoB (apolipoprotein B)-containing lipoprotein particles, such as chylomicrons, very-low-density and low-density lipoprotein particles, transport triacylglycerol and cholesteryl esters in the bloodstream. A palmitoylation site was previously mapped to Cys-1085 in a functional truncated apoB variant (apoB-29) and abolished by mutagenesis. This Cys-1085Ser mutation resulted in secretion of smaller and denser lipoprotein particles containing 80% less cholesteryl ester and triacylglycerol than wild-type controls. We show that palmitoylation of apoB-29 occurs in the ER (endoplasmic reticulum), stimulates the ER-Golgi transport rate of apoB-29 almost 2-fold, doubles the secretion efficiency of wild-type apoB-29 in comparison with (Cys-1085Ser)apoB-29 and reduces significantly the association of wild-type apoB-29 with calnexin in comparison with (Cys-1085Ser)apoB-29. While non-palmitoylated apoB-29 co-localized extensively with constitutively secreted transferrin, wild-type apoB-29 did so only partially and was enriched in ER extensions. Our results suggest that palmitoylation of apoB regulates the biogenesis of nascent apoB-containing lipoprotein particles by concentrating apoB in a specialized ER compartment and by stimulating dissociation from constituents of the ER quality-control machinery. This reduced interaction would lead to a faster ER-Golgi transit time and a higher secretion efficiency of wild-type apoB-29. Palmitoylation could regulate the amount of apoB available for secretion of neutral lipids.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/14498830-10428023,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/14498830-9843958
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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 |
1470-8728
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
377
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
121-30
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:14498830-Animals,
pubmed-meshheading:14498830-Apolipoproteins B,
pubmed-meshheading:14498830-Cell Line, Tumor,
pubmed-meshheading:14498830-Cysteine,
pubmed-meshheading:14498830-Endoplasmic Reticulum,
pubmed-meshheading:14498830-Golgi Apparatus,
pubmed-meshheading:14498830-Humans,
pubmed-meshheading:14498830-Mutation,
pubmed-meshheading:14498830-Palmitic Acids,
pubmed-meshheading:14498830-Protein Folding,
pubmed-meshheading:14498830-Rats
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pubmed:year |
2004
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pubmed:articleTitle |
A role for palmitoylation in the quality control, assembly and secretion of apolipoprotein B.
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pubmed:affiliation |
Department of Cell Biology, Faculty of Medicine and Dentistry, University of Alberta, 555 Medical Science Building, Edmonton, Alberta, Canada T6G 2H7.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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