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Journal of Lipid Research, Vol. 44, 22-32, January 2003
Copyright © 2003 by Lipid Research, Inc.
Review |
* Departments of Anatomy and Cell Biology, SUNY Downstate Medical Center, 450 Clarkson Avenue, , Brooklyn, NY 11203
Pediatrics, SUNY Downstate Medical Center, 450 Clarkson Avenue, , Brooklyn, NY 11203
Medicine Biophysics Division, SUNY Downstate Medical Center, 450 Clarkson Avenue, , Brooklyn, NY 11203
1 To whom correspondence should be addressed. e-mail: mahmood.hussain{at}downstate.edu
Apolipoprotein B (apoB) and microsomal triglyceride transfer protein (MTP) are necessary for lipoprotein assembly. ApoB consists of five structural domains, ß
1-ß1-2-ß2-3. We propose that MTP contains three structural motifs (N-terminal ß-barrel, central -helix, and C-terminal lipid cavity) and three functional domains (lipid transfer, membrane associating, and apoB binding). MTP's lipid transfer activity is required for the assembly of lipoproteins. This activity renders nascent apoB secretion-competent and may be involved in the import of triglycerides into the lumen of endoplasmic reticulum. In addition, MTP binds to apoB with high affinity involving ionic interactions. MTP interacts at multiple sites in the N-terminal ß1 structural domain of apoB. A novel antagonist that inhibits apoB-MTP binding decreases apoB secretion. Furthermore, site-directed mutagenesis and deletion analyses that inhibit apoB-MTP binding decrease apoB secretion. Lipids modulate protein-protein interactions between apoB and MTP. Lipids associated with MTP increase apoB-MTP binding whereas lipids associated with apoB decrease this binding. Thus, specific antagonist, site-directed mutagenesis, deletion analyses, and modulation studies support the notion that apoB-MTP binding plays a role in lipoprotein biogenesis. However, specific steps in lipoprotein assembly that require apoB-MTP binding have not been identified.
ApoB-MTP binding may be important for the prevention of degradation and lipidation of nascent apoB.
Abbreviations: ER, endoplasmic reticulum; MTP, microsomal tri-glyceride transfer protein; M subunit, 97-kDa subunit of the MTP complex; P subunit, the 55-kDa PDI subunit of the MTP complex; PDI, protein disulfide isomerase
Supplementary key words protein-protein interactions • protein motifs • domains • abetalipoproteinemia • hypobetalipoproteinemia • apolipoprotein B • MTP
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