The tetraspanin CD63/lamp3 cycles between endocytic and secretory compartments in human endothelial cells

Kobayashi, Toshihide, Vischer, Ulrich M., Rosnoblet, Corinne, Lebrand, Cecile, Lindsay, Margaret, Parton, Robert G., Kruithof, Egbert K. O. and Gruenberg, Jean (2000) The tetraspanin CD63/lamp3 cycles between endocytic and secretory compartments in human endothelial cells. Molecular Biology of the Cell, 11 5: 1829-1843.

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Author Kobayashi, Toshihide
Vischer, Ulrich M.
Rosnoblet, Corinne
Lebrand, Cecile
Lindsay, Margaret
Parton, Robert G.
Kruithof, Egbert K. O.
Gruenberg, Jean
Title The tetraspanin CD63/lamp3 cycles between endocytic and secretory compartments in human endothelial cells
Journal name Molecular Biology of the Cell   Check publisher's open access policy
ISSN 1059-1524
Publication date 2000-05-01
Sub-type Article (original research)
Open Access Status File (Publisher version)
Volume 11
Issue 5
Start page 1829
End page 1843
Total pages 15
Place of publication Bethesda, MD, United States
Publisher American Society for Cell Biology
Language eng
Abstract In the present study, we show that in human endothelial cells the tetraspanin CD63/lamp3 distributes predominantly to the internal membranes of multivesicular-multilamellar late endosomes, which contain the unique lipid lysobisphosphatidic acid. Some CD63/lamp3 is also present in Weibel-Palade bodies, the characteristic secretory organelle of these cells. We find that CD63/lamp3 molecules can be transported from late endosomes to Weibel-Palade bodies and thus that CD63/lamp3 cycles between endocytic and biosynthetic compartments; however, movement of CD63/lamp3 is much slower than that of P- selectin, which is known to cycle between plasma membrane and Weibel-Palade bodies. When cells are treated with U18666A, a drug that mimics the Niemann- Pick type C syndrome, both proteins accumulate in late endosomes and fail to reach Weibel-Palade bodies efficiently, suggesting that P-selectin, like CD63/lamp3, cycles via late endosomes. Our data suggest that CD63/lamp3 partitions preferentially within late endosome internal membranes, thus causing its accumulation, and that this mechanism contributes to CD63/lamp3 retention in late endosomes; however, our data also indicate that the protein can eventually escape from these internal membranes and recycle toward Weibel-Palade bodies to be reused. Our observations thus uncover the existence of a selective trafficking route from late endosomes to Weibel- Palade bodies.
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Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
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