期刊
MOLECULAR BIOLOGY OF THE CELL
卷 22, 期 23, 页码 4621-4634出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E11-04-0320
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资金
- Agence Nationale de la Recherche [05-BLAN 296-01]
- European Union [222887]
- Comision Nacional de Investigacion Cientifica y Tecnologica (Chile)/Basal [PFB 12/2007]
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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