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Interaction abolishment between mutant caveolin-1(Delta 62-100) and ABCA1 reduces HDL-mediated cellular cholesterol efflux

  作者 Kuo, CY; Lin, YC; Yang, JJ; Yang, VC  
  选自 期刊  Biochemical and Biophysical Research Communications;  卷期  2011年414-2;  页码  337-343  
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[摘要]Our previous study shows that caveolin-1 colocalizes and interacts with ATP-binding cassette transporter A1 (ABCA1), which is intimately involved in cellular cholesterol efflux. In this study, we further clarified the region of caveolin-1 that interacts with ABCA1. We also examined the interaction between mutant caveolin-1 and ABCA1 in HDL-mediated cholesterol efflux. We constructed a panel of mutant caveolin-1 proteins and co-transfected them into rat aortic endothelial and human embryonic kidney 293 (HEK293) cells. The co-immunoprecipitation shows that mutant oligomerization domain of caveolin-1, caveolin-1(Delta 62-100), is required for the interaction of caveolin-1 with ABCA1. Caveolin-1(Delta 62-100) did not colocalize with ABCA1 in the cholesterol-loaded cells after HDL incubation as observed by immunofluorescence confocal microscopy. Concomitantly, caveolin-1(Delta 62-100) suppressed HDL-mediated cholesterol efflux. The results suggest that the region of caveolin-1 between amino acids 62 and 100 is an oligomerization domain as well as an attachment site for ABCA1 interaction that regulates HDL-mediated cholesterol efflux. (C) 2011 Elsevier Inc. All rights reserved.

 
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