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Modulation of Cellular Cholesterol Transport and Homeostasis by Rab11

Hölttä-Vuori, Maarit, Tanhuanpää, Kimmo, Möbius, Wiebke, Somerharju, Pentti, Ikonen, Elina·2002·Molecular Biology of the Cell
DOI 10.1091/mbc.e02-01-0025
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Abstract

To analyze the contribution of vesicular trafficking pathways in cellular cholesterol transport we examined the effects of selected endosomal Rab proteins on cholesterol distribution by filipin staining. Transient overexpression of Rab11 resulted in prominent accumulation of free cholesterol in Rab11-positive organelles that sequestered transferrin receptors and internalized transferrin. Sphingolipids were selectively redistributed as pyrene-sphingomyelin and sulfatide cosequestered with Rab11-positive endosomes, whereas globotriaosyl ceramide and GM2 ganglioside did not. Rab11 overexpression did not perturb the transport of 1,1′-dioctadecyl-3,3,3′,3′-tetramethyl-indocarbocyanine-perchlorate–labeled low-density lipoprotein (LDL) to late endosomes or the Niemann-Pick type C1 (NPC1)-induced late endosomal cholesterol clearance in NPC patient cells. However, Rab11 overexpression inhibited cellular cholesterol esterification in an LDL-independent manner. This effect could be overcome by introducing cholesterol to the plasma membrane by using cyclodextrin as a carrier. These results suggest that in Rab11-overexpressing cells, deposition of cholesterol in recycling endosomes results in its impaired esterification, presumably due to defective recycling of cholesterol to the plasma membrane. The findings point to the importance of the recycling endosomes in regulating cholesterol and sphingolipid trafficking and cellular cholesterol homeostasis.

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  • EHD1 plays a critical role in recycling of plasma membrane receptors (e.g., transferrin) internalized through clathrin-coated pits or independently of clathrin.

    “EHD1 [14] has been found to play a critical role in the recycling of plasma membrane receptors (ie., transferrin) that are internalized either through clathrin-coated pits [15-17], or independently of clathrin (MHC-I or β1 integrins) [18,19].”

    From EHD1 regulates cholesterol homeostasis and lipid droplet storage (2007) · cites this paper as [15]

  • Re-introduction of wild-type EHD1, but not dysfunctional EHD1 mutants, restores free cholesterol levels in Ehd1-/- MEFs.

    “returned to normal level upon re-introduction of wild-type, but not dysfunctional EHD1”

    From EHD1 regulates cholesterol homeostasis and lipid droplet storage (2007) · cites this paper as [15]

  • The EHD1 mutants Myc-EHD1 ΔEH and Myc-EHD1 G65R are dysfunctional.

    “two previously described dysfunctional EHD1 mutants, Myc-EHD1 ΔEH and Myc-EHD1 G65R (Fig. 2D-G; stars)[15,18]”

    From EHD1 regulates cholesterol homeostasis and lipid droplet storage (2007) · cites this paper as [15]

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Metadata

Authors
Hölttä-Vuori, M., Tanhuanpää, K., Möbius, W., Somerharju, P., & Ikonen, E.
Affiliations
  • Department of Molecular Medicine, National Public Health Institute, Biomedicum Helsinki, 00251 Helsinki, Finland;
  • Department of Cell Biology, University Medical Center Utrecht and Center for Biomedical Genetics, 3584 CX Utrecht, The Netherlands; and
  • Institute of Biomedicine, University of Helsinki, Helsinki, Finland
Venue
Molecular Biology of the Cell
Publisher
American Society for Cell Biology (ASCB)
Published
2002-09
Volume
13
Issue
9
Pages
3107-3122
ISSN
  • 1059-1524
  • 1939-4586
DOI
10.1091/mbc.e02-01-0025
Cited by
120
References
2
Language
en

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