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© Research
Publication : Molecular biology of the cell

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Molecular biology of the cell - 12 Oct 2011

Imjeti NS, Lebreton S, Paladino S, de la Fuente E, Gonzalez A, Zurzolo C

Link to Pubmed [PMID] – 21998201

Mol. Biol. Cell 2011 Dec;22(23):4621-34

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.