N-Glycosylation instead of cholesterol mediates oligomerization and apical sorting of GPI-APs in FRT cells. - Archive ouverte HAL Access content directly
Journal Articles Molecular Biology of the Cell Year : 2011

N-Glycosylation instead of cholesterol mediates oligomerization and apical sorting of GPI-APs in FRT cells.

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Abstract

Sorting of glycosylphosphatidyl-inositol--anchored proteins (GPI-APs) in polarized epithelial cells is not fully understood. Oligomerization in the Golgi complex has emerged as the crucial event driving apical segregation of GPI-APs in two different kind of epithelial cells, Madin-Darby canine kidney (MDCK) and Fisher rat thyroid (FRT) cells, but whether the mechanism is conserved is unknown. In MDCK cells cholesterol promotes GPI-AP oligomerization, as well as apical sorting of GPI-APs. Here we show that FRT cells lack this cholesterol-driven oligomerization as apical sorting mechanism. In these cells both apical and basolateral GPI-APs display restricted diffusion in the Golgi likely due to a cholesterol-enriched membrane environment. It is striking that N-glycosylation is the critical event for oligomerization and apical sorting of GPI-APs in FRT cells but not in MDCK cells. Our data indicate that at least two mechanisms exist to determine oligomerization in the Golgi leading to apical sorting of GPI-APs. One depends on cholesterol, and the other depends on N-glycosylation and is insensitive to cholesterol addition or depletion.
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pasteur-00663149 , version 1 (03-02-2012)

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Naga Salaija Imjeti, Stéphanie Lebreton, Simona Paladino, Erwin de La Fuente, Alfonso Gonzalez, et al.. N-Glycosylation instead of cholesterol mediates oligomerization and apical sorting of GPI-APs in FRT cells.. Molecular Biology of the Cell, 2011, 22 (23), pp.4621-34. ⟨10.1091/mbc.E11-04-0320⟩. ⟨pasteur-00663149⟩
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