A common binding site on the microsomal triglyceride transfer protein for apolipoprotein B and protein disulfide isomerase

被引:80
作者
Bradbury, P
Mann, CJ
Köchl, S
Anderson, TA
Chester, SA
Hancock, JM
Ritchie, PJ
Amey, J
Harrison, GB
Levitt, DG
Banaszak, LJ
Scott, J
Shoulders, CC
机构
[1] Univ London Imperial Coll Sci Technol & Med, Hammersmith Hosp, Ctr Clin Sci, MRC Mol Med Grp, London W12 0NN, England
[2] Univ London Imperial Coll Sci Technol & Med, Hammersmith Hosp, Ctr Clin Sci, Gene Genome Evolut Grp, London W12 0NN, England
[3] Univ London Imperial Coll Sci Technol & Med, Hammersmith Hosp, Natl Heart & Lung Inst, London W12 0NN, England
[4] Inst Gerichtliche Med, A-6020 Innsbruck, Austria
[5] Univ Minnesota, Sch Med, Dept Biochem, Minneapolis, MN 55455 USA
关键词
D O I
10.1074/jbc.274.5.3159
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 aminoterminal 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 coimmunoprecipitation. 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.
引用
收藏
页码:3159 / 3164
页数:6
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